The Enzyme Database

Displaying entries 151-200 of 485.

<< Previous | Next >>    printer_iconPrintable version

EC 2.3.1.201     
Accepted name: UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase
Reaction: acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate = CoA + UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Other name(s): WbpD; WlbB
Systematic name: acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate N-acetyltransferase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854–11862. [DOI] [PMID: 19282284]
2.  Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446–5455. [DOI] [PMID: 19348502]
[EC 2.3.1.201 created 2012]
 
 
EC 2.3.1.203     
Accepted name: UDP-N-acetylbacillosamine N-acetyltransferase
Reaction: acetyl-CoA + UDP-N-acetylbacillosamine = CoA + UDP-N,N′-diacetylbacillosamine
For diagram of legionaminic acid biosynthesis, click here
Glossary: UDP-N-acetylbacillosamine = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine
UDP-N,N′-diacetylbacillosamine = UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose
Other name(s): UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase; pglD (gene name)
Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine N-acetyltransferase
Comments: The product, UDP-N,N′-diacetylbacillosamine, is an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [1,2] and O-linked glycosylation of certain L-serine residues in Neisseria species [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520]
2.  Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827–1836. [DOI] [PMID: 18198901]
3.  Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N′-diacetylbacillosamine. Biochemistry 50 (2011) 4936–4948. [DOI] [PMID: 21542610]
[EC 2.3.1.203 created 2012, modified 2013]
 
 
EC 2.3.1.224     
Accepted name: acetyl-CoA-benzylalcohol acetyltransferase
Reaction: (1) acetyl-CoA + benzyl alcohol = CoA + benzyl acetate
(2) acetyl-CoA + cinnamyl alcohol = CoA + cinnamyl acetate
Other name(s): BEAT
Systematic name: acetyl-CoA:benzylalcohol O-acetyltransferase
Comments: The enzyme is found in flowers like Clarkia breweri, where it is important for floral scent production. Unlike EC 2.3.1.84, alcohol O-acetyltransferase, this enzyme is active with alcohols that contain a benzyl ring.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dudareva, N., D'Auria, J.C., Nam, K.H., Raguso, R.A. and Pichersky, E. Acetyl-CoA:benzylalcohol acetyltransferase - an enzyme involved in floral scent production in Clarkia breweri. Plant J. 14 (1998) 297–304. [DOI] [PMID: 9628024]
[EC 2.3.1.224 created 2013]
 
 
EC 2.3.1.226     
Accepted name: carboxymethylproline synthase
Reaction: malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O = CoA + (2S,5S)-5-carboxymethylproline + CO2
Other name(s): CarB (ambiguous)
Systematic name: malonyl-CoA:(S)-1-pyrroline-5-carboxylate malonyltransferase (cyclizing)
Comments: The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sleeman, M.C. and Schofield, C.J. Carboxymethylproline synthase (CarB), an unusual carbon-carbon bond-forming enzyme of the crotonase superfamily involved in carbapenem biosynthesis. J. Biol. Chem. 279 (2004) 6730–6736. [DOI] [PMID: 14625287]
2.  Gerratana, B., Arnett, S.O., Stapon, A. and Townsend, C.A. Carboxymethylproline synthase from Pectobacterium carotorova: a multifaceted member of the crotonase superfamily. Biochemistry 43 (2004) 15936–15945. [DOI] [PMID: 15595850]
3.  Sorensen, J.L., Sleeman, M.C. and Schofield, C.J. Synthesis of deuterium labelled L- and D-glutamate semialdehydes and their evaluation as substrates for carboxymethylproline synthase (CarB)—implications for carbapenem biosynthesis. Chem. Commun. (Camb.) (2005) 1155–1157. [DOI] [PMID: 15726176]
4.  Sleeman, M.C., Sorensen, J.L., Batchelar, E.T., McDonough, M.A. and Schofield, C.J. Structural and mechanistic studies on carboxymethylproline synthase (CarB), a unique member of the crotonase superfamily catalyzing the first step in carbapenem biosynthesis. J. Biol. Chem. 280 (2005) 34956–34965. [DOI] [PMID: 16096274]
5.  Batchelar, E.T., Hamed, R.B., Ducho, C., Claridge, T.D., Edelmann, M.J., Kessler, B. and Schofield, C.J. Thioester hydrolysis and C-C bond formation by carboxymethylproline synthase from the crotonase superfamily. Angew. Chem. Int. Ed. Engl. 47 (2008) 9322–9325. [DOI] [PMID: 18972478]
6.  Hamed, R.B., Gomez-Castellanos, J.R., Thalhammer, A., Harding, D., Ducho, C., Claridge, T.D. and Schofield, C.J. Stereoselective C-C bond formation catalysed by engineered carboxymethylproline synthases. Nat. Chem. 3 (2011) 365–371. [DOI] [PMID: 21505494]
[EC 2.3.1.226 created 2013]
 
 
EC 2.3.1.230     
Accepted name: 2-heptyl-4(1H)-quinolone synthase
Reaction: octanoyl-CoA + (2-aminobenzoyl)acetate = 2-heptyl-4-quinolone + CoA + CO2 + H2O (overall reaction)
(1a) octanoyl-CoA + L-cysteinyl-[PqsC protein] = S-octanoyl-L-cysteinyl-[PqsC protein] + CoA
(1b) S-octanoyl-L-cysteinyl-[PqsC protein] + (2-aminobenzoyl)acetate = 1-(2-aminophenyl)decane-1,3-dione + CO2 + L-cysteinyl-[PqsC protein]
(1c) 1-(2-aminophenyl)decane-1,3-dione = 2-heptyl-4-quinolone + H2O
Glossary: 2-heptyl-4-quinolone = 2-heptylquinolin-4(1H)-one
Other name(s): pqsBC (gene names); malonyl-CoA:anthraniloyl-CoA C-acetyltransferase (decarboxylating)
Systematic name: octanoyl-CoA:(2-aminobenzoyl)acetate octanoyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, is a heterodimeric complex. The PqsC subunit acquires an octanoyl group from octanoyl-CoA and attaches it to an internal cysteine residue. Together with the PqsB subunit, the proteins catalyse the coupling of the octanoyl group with (2-aminobenzoyl)acetate, leading to decarboxylation and dehydration events that result in closure of the quinoline ring.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481–1491. [DOI] [PMID: 24239007]
2.  Drees, S.L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J. and Fetzner, S. PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. J. Biol. Chem. 291 (2016) 6610–6624. [DOI] [PMID: 26811339]
[EC 2.3.1.230 created 2013, modified 2017]
 
 
EC 2.3.1.231     
Accepted name: tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methoxycarbonyltransferase
Reaction: S-adenosyl-L-methionine + 7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe + CO2 = S-adenosyl-L-homocysteine + wybutosine37 in tRNAPhe
For diagram of wyosine biosynthesis, click here
Glossary: wyosine = 4,6-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
wybutosine = yW = 7-{(3S)-3-(methoxycarbonyl)-3-(methoxycarbonylamino)propyl}-4,5-dimethyl-3-(β-D-ribofuranosyl)-3,4-dihydro-9H-imidazo[1,2-a]purin-9-one
Other name(s): TYW4 (ambiguous); tRNA-yW synthesizing enzyme-4 (ambiguous)
Systematic name: S-adenosyl-L-methionine:tRNAPhe {7-[(3S)-3-amino-3-(methoxycarbonyl)propyl]wyosine37-N}-methyltransferase (carbon dioxide-adding)
Comments: The enzyme is found only in eukaryotes, where it is involved in the biosynthesis of wybutosine, a hypermodified tricyclic base found at position 37 of certain tRNAs. The modification is important for translational reading-frame maintenance. In some species that produce hydroxywybutosine the enzyme uses 7-[2-hydroxy-3-amino-3-(methoxycarbonyl)propyl]wyosine37 in tRNAPhe as substrate. The enzyme also has the activity of EC 2.1.1.290, tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Noma, A., Kirino, Y., Ikeuchi, Y. and Suzuki, T. Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J. 25 (2006) 2142–2154. [DOI] [PMID: 16642040]
2.  Suzuki, Y., Noma, A., Suzuki, T., Ishitani, R. and Nureki, O. Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4. Nucleic Acids Res. 37 (2009) 2910–2925. [DOI] [PMID: 19287006]
3.  Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and Nureki, O. Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification. Nucleic Acids Res. 39 (2011) 1576–1585. [DOI] [PMID: 20972222]
[EC 2.3.1.231 created 2013]
 
 
EC 2.3.1.232     
Accepted name: methanol O-anthraniloyltransferase
Reaction: anthraniloyl-CoA + methanol = CoA + O-methyl anthranilate
Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA
Other name(s): AMAT; anthraniloyl-coenzyme A (CoA):methanol acyltransferase
Systematic name: anthraniloyl-CoA:methanol O-anthraniloyltransferase
Comments: The enzyme from Concord grape (Vitis labrusca) is solely responsible for the production of O-methyl anthranilate, an important aroma and flavor compound in the grape. The enzyme has a broad substrate specificity, and can use a range of alcohols with substantial activity, the best being butanol, benzyl alcohol, iso-pentanol, octanol and 2-propanol. It can use benzoyl-CoA and acetyl-CoA as acyl donors with lower efficiency. In addition to O-methyl anthranilate, the enzyme might be responsible for the production of ethyl butanoate, methyl-3-hydroxy butanoate and ethyl-3-hydroxy butanoate, which are present in large quantities in the grapes. Also catalyses EC 2.3.1.196, benzyl alcohol O-benzoyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, J. and De Luca, V. The biosynthesis and regulation of biosynthesis of Concord grape fruit esters, including ’foxy’ methylanthranilate. Plant J. 44 (2005) 606–619. [DOI] [PMID: 16262710]
[EC 2.3.1.232 created 2014]
 
 
EC 2.3.1.254     
Accepted name: N-terminal methionine Nα-acetyltransferase NatB
Reaction: (1) acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-asparaginyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-aspartyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal Nα-acetyl-L-methionyl-L-glutamyl-[protein] + CoA
Other name(s): NAA20 (gene name); NAA25 (gene name)
Systematic name: acetyl-CoA:N-terminal Met-Asn/Gln/Asp/Glu-[protein] Met-Nα-acetyltransferase
Comments: N-terminal acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Starheim, K.K., Arnesen, T., Gromyko, D., Ryningen, A., Varhaug, J.E. and Lillehaug, J.R. Identification of the human Nα-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression. Biochem. J. 415 (2008) 325–331. [DOI] [PMID: 18570629]
2.  Ferrandez-Ayela, A., Micol-Ponce, R., Sanchez-Garcia, A.B., Alonso-Peral, M.M., Micol, J.L. and Ponce, M.R. Mutation of an Arabidopsis NatB N-α-terminal acetylation complex component causes pleiotropic developmental defects. PLoS One 8:e80697 (2013). [DOI] [PMID: 24244708]
3.  Lee, K.E., Ahn, J.Y., Kim, J.M. and Hwang, C.S. Synthetic lethal screen of NAA20, a catalytic subunit gene of NatB N-terminal acetylase in Saccharomyces cerevisiae. J Microbiol 52 (2014) 842–848. [DOI] [PMID: 25163837]
[EC 2.3.1.254 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.254]
 
 
EC 2.3.1.256     
Accepted name: N-terminal methionine Nα-acetyltransferase NatC
Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
Other name(s): NAA30 (gene name); NAA35 (gene name); NAA38 (gene name); MAK3 (gene name); MAK10 (gene name); MAK31 (gene name)
Systematic name: acetyl-CoA:N-terminal-Met-Leu/Ile/Phe/Trp/Tyr-[protein] Met Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Polevoda, B. and Sherman, F. NatC Nα-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p. J. Biol. Chem. 276 (2001) 20154–20159. [DOI] [PMID: 11274203]
2.  Polevoda, B. and Sherman, F. Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 308 (2003) 1–11. [DOI] [PMID: 12890471]
3.  Pesaresi, P., Gardner, N.A., Masiero, S., Dietzmann, A., Eichacker, L., Wickner, R., Salamini, F. and Leister, D. Cytoplasmic N-terminal protein acetylation is required for efficient photosynthesis in Arabidopsis. Plant Cell 15 (2003) 1817–1832. [DOI] [PMID: 12897255]
4.  Wenzlau, J.M., Garl, P.J., Simpson, P., Stenmark, K.R., West, J., Artinger, K.B., Nemenoff, R.A. and Weiser-Evans, M.C. Embryonic growth-associated protein is one subunit of a novel N-terminal acetyltransferase complex essential for embryonic vascular development. Circ. Res. 98 (2006) 846–855. [DOI] [PMID: 16484612]
5.  Starheim, K.K., Gromyko, D., Evjenth, R., Ryningen, A., Varhaug, J.E., Lillehaug, J.R. and Arnesen, T. Knockdown of human Nα-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell Biol. 29 (2009) 3569–3581. [DOI] [PMID: 19398576]
[EC 2.3.1.256 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.256]
 
 
EC 2.3.1.258     
Accepted name: N-terminal methionine Nα-acetyltransferase NatE
Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-alanyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-seryl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-seryl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-valyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-valyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-threonyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-threonyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-lysyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-lysyl-[protein] + CoA
(6) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(7) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
(8) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosyl-[protein] + CoA
Other name(s): NAA50 (gene name); NAT5; SAN
Systematic name: acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nα-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hou, F., Chu, C.W., Kong, X., Yokomori, K. and Zou, H. The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner. J. Cell Biol. 177 (2007) 587–597. [DOI] [PMID: 17502424]
2.  Pimenta-Marques, A., Tostoes, R., Marty, T., Barbosa, V., Lehmann, R. and Martinho, R.G. Differential requirements of a mitotic acetyltransferase in somatic and germ line cells. Dev. Biol. 323 (2008) 197–206. [DOI] [PMID: 18801358]
3.  Evjenth, R., Hole, K., Karlsen, O.A., Ziegler, M., Arnesen, T. and Lillehaug, J.R. Human Naa50p (Nat5/San) displays both protein Nα- and Nε-acetyltransferase activity. J. Biol. Chem. 284 (2009) 31122–31129. [DOI] [PMID: 19744929]
4.  Van Damme, P., Hole, K., Gevaert, K. and Arnesen, T. N-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases. Proteomics 15 (2015) 2436–2446. [DOI] [PMID: 25886145]
[EC 2.3.1.258 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.258]
 
 
EC 2.3.1.259     
Accepted name: N-terminal methionine Nα-acetyltransferase NatF
Reaction: acetyl-CoA + an N-terminal-L-methionyl-[transmembrane protein] = an N-terminal-Nα-acetyl-L-methionyl-[transmembrane protein] + CoA
Other name(s): NAA60 (gene name)
Systematic name: acetyl-CoA:N-terminal-Met-Lys/Ser/Val/Leu/Gln/Ile/Tyr/Thr-[transmembrane protein] Met-Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. NatF is found only in higher eukaryotes, and is absent from yeast. Unlike other Nat systems the enzyme is located in the Golgi apparatus. It faces the cytosolic side of intracellular membranes, and specifically acetylates transmembrane proteins whose N termini face the cytosol. NatF targets N-terminal L-methionine residues attached to Lys, Ser, Val, Leu, Gln, Ile, Tyr and Thr residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Van Damme, P., Hole, K., Pimenta-Marques, A., Helsens, K., Vandekerckhove, J., Martinho, R.G., Gevaert, K. and Arnesen, T. NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 7:e1002169 (2011). [DOI] [PMID: 21750686]
2.  Aksnes, H., Van Damme, P., Goris, M., Starheim, K.K., Marie, M., Støve, S.I., Hoel, C., Kalvik, T.V., Hole, K., Glomnes, N., Furnes, C., Ljostveit, S., Ziegler, M., Niere, M., Gevaert, K. and Arnesen, T. An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. Cell Rep. 10 (2015) 1362–1374. [DOI] [PMID: 25732826]
[EC 2.3.1.259 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.259]
 
 
EC 2.3.1.260     
Accepted name: tetracycline polyketide synthase
Reaction: malonamoyl-[OxyC acyl-carrier protein] + 8 malonyl-CoA = 18-carbamoyl-3,5,7,9,11,13,15,17-octaoxooctadecanoyl-[OxyC acyl-carrier protein] + 8 CO2 + 8 CoA
For diagram of tetracycline biosynthesis, click here
Systematic name: malonyl-CoA:malonamoyl-[OxyC acyl-carrier protein] malonyltransferase
Comments: The synthesis, in the bacterium Streptomyces rimosus, of the tetracycline antibiotics core skeleton requires a minimal polyketide synthase (PKS) consisting of a ketosynthase (KS), a chain length factor (CLF), and an acyl-carrier protein (ACP). Initiation involves an amide-containing starter unit that becomes the C-2 amide that is present in the tetracycline compounds. Following the initiation, the PKS catalyses the iterative condensation of 8 malonyl-CoA molecules to yield the polyketide backbone of tetracycline. Throughout the proccess, the nascent chain is attached to the OxyC acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Thomas, R. and Williams, D.J. Oxytetracycline biosynthesis: origin of the carboxamide substituent. J. Chem. Soc., Chem. Commun. (1983) 677–679.
2.  Zhang, W., Ames, B.D., Tsai, S.C. and Tang, Y. Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase. Appl. Environ. Microbiol. 72 (2006) 2573–2580. [DOI] [PMID: 16597959]
3.  Yu, L., Cao, N., Wang, L., Xiao, C., Guo, M., Chu, J., Zhuang, Y. and Zhang, S. Oxytetracycline biosynthesis improvement in Streptomyces rimosus following duplication of minimal PKS genes. Enzyme Microb. Technol. 50 (2012) 318–324. [DOI] [PMID: 22500899]
[EC 2.3.1.260 created 2016]
 
 
EC 2.3.1.262     
Accepted name: anthraniloyl-CoA anthraniloyltransferase
Reaction: anthraniloyl-CoA + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CoA + CO2 (overall reaction)
(1a) anthraniloyl-CoA + L-cysteinyl-[PqsD protein] = S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
(1b) S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA = (2-aminobenzoyl)acetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]
Glossary: anthraniloyl-CoA = 2-aminobenzoyl-CoA
Other name(s): pqsD (gene name)
Systematic name: anthraniloyl-CoA:malonyl-CoA anthraniloyltransferase
Comments: The enzyme, characterized from the bacterium Pseudomonas aeruginosa, participates in the synthesis of the secondary metabolites 2-heptyl-3-hydroxy-4(1H)-quinolone and 4-hydroxy-2(1H)-quinolone. The enzyme transfers an anthraniloyl group from anthraniloyl-CoA to an internal L-cysteine residue, followed by its transfer to malonyl-CoA to produce a short-lived product that can cyclize spontaneously to form 4-hydroxy-2(1H)-quinolone. However, when EC 3.1.2.32, 2-aminobenzoylacetyl-CoA thioesterase, is present, it removes the CoA moiety from the product, forming the stable (2-aminobenzoyl)acetate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bera, A.K., Atanasova, V., Robinson, H., Eisenstein, E., Coleman, J.P., Pesci, E.C. and Parsons, J.F. Structure of PqsD, a Pseudomonas quinolone signal biosynthetic enzyme, in complex with anthranilate. Biochemistry 48 (2009) 8644–8655. [DOI] [PMID: 19694421]
2.  Dulcey, C.E., Dekimpe, V., Fauvelle, D.A., Milot, S., Groleau, M.C., Doucet, N., Rahme, L.G., Lepine, F. and Deziel, E. The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. Chem. Biol. 20 (2013) 1481–1491. [DOI] [PMID: 24239007]
3.  Drees, S.L. and Fetzner, S. PqsE of Pseudomonas aeruginosa acts as pathway-specific thioesterase in the biosynthesis of alkylquinolone signaling molecules. Chem. Biol. 22 (2015) 611–618. [DOI] [PMID: 25960261]
[EC 2.3.1.262 created 2017]
 
 
EC 2.3.1.294     
Accepted name: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II
Reaction: an ultra-long-chain di-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = an ultra-long-chain di-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + a holo-[acyl-carrier protein]
Other name(s): kasB (gene name); β-ketoacyl-acyl carrier protein synthase KasB
Systematic name: ultra-long-chain di-unsaturated fattyl acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Comments: The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasB differs from KasA (EC 2.3.1.293, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I), by preferring longer substrates (closer to the upper limit), which also contain two double bonds.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schaeffer, M.L., Agnihotri, G., Volker, C., Kallender, H., Brennan, P.J. and Lonsdale, J.T. Purification and biochemical characterization of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases KasA and KasB. J. Biol. Chem. 276 (2001) 47029–47037. [PMID: 11600501]
2.  Gao, L.Y., Laval, F., Lawson, E.H., Groger, R.K., Woodruff, A., Morisaki, J.H., Cox, J.S., Daffe, M. and Brown, E.J. Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy. Mol. Microbiol. 49 (2003) 1547–1563. [PMID: 12950920]
3.  Molle, V., Brown, A.K., Besra, G.S., Cozzone, A.J. and Kremer, L. The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J. Biol. Chem. 281 (2006) 30094–30103. [PMID: 16873379]
4.  Bhatt, A., Fujiwara, N., Bhatt, K., Gurcha, S.S., Kremer, L., Chen, B., Chan, J., Porcelli, S.A., Kobayashi, K., Besra, G.S. and Jacobs, W.R., Jr. Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. Proc. Natl. Acad. Sci. USA 104 (2007) 5157–5162. [PMID: 17360388]
5.  Yamada, H., Bhatt, A., Danev, R., Fujiwara, N., Maeda, S., Mitarai, S., Chikamatsu, K., Aono, A., Nitta, K., Jacobs, W.R., Jr. and Nagayama, K. Non-acid-fastness in Mycobacterium tuberculosis Δ kasB mutant correlates with the cell envelope electron density. Tuberculosis (Edinb) 92 (2012) 351–357. [PMID: 22516756]
6.  Vilcheze, C., Molle, V., Carrere-Kremer, S., Leiba, J., Mourey, L., Shenai, S., Baronian, G., Tufariello, J., Hartman, T., Veyron-Churlet, R., Trivelli, X., Tiwari, S., Weinrick, B., Alland, D., Guerardel, Y., Jacobs, W.R., Jr. and Kremer, L. Phosphorylation of KasB regulates virulence and acid-fastness in Mycobacterium tuberculosis. PLoS Pathog. 10:e1004115 (2014). [PMID: 24809459]
[EC 2.3.1.294 created 2019]
 
 
EC 2.3.1.299     
Accepted name: sphingoid base N-stearoyltransferase
Reaction: stearoyl-CoA + a sphingoid base = an N-(stearoyl)-sphingoid base + CoA
Glossary: a sphingoid base = an amino alcohol, composed predominantly of 18 carbon atoms, characterized by the presence of a hydroxyl group at C-1 (and often also at C-3), and an amine group at C-2.
Other name(s): mammalian ceramide synthase 1; LASS1 (gene name); UOG1 (gene name); CERS1 (gene name)
Systematic name: stearoyl-CoA:sphingoid base N-stearoyltransferase
Comments: Mammals have six ceramide synthases that exhibit relatively strict specificity regarding the chain-length of their acyl-CoA substrates. Ceramide synthase 1 (CERS1) is structurally and functionally distinctive from all other CERS enzymes, and is specific for stearoyl-CoA as the acyl donor. It can use multiple sphingoid bases including sphinganine, sphingosine, and phytosphingosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Venkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J.C., Sullards, M.C., Merrill, A.H., Jr. and Futerman, A.H. Upstream of growth and differentiation factor 1 (uog1), a mammalian homolog of the yeast longevity assurance gene 1 (LAG1), regulates N-stearoyl-sphinganine (C18-(dihydro)ceramide) synthesis in a fumonisin B1-independent manner in mammalian cells. J. Biol. Chem. 277 (2002) 35642–35649. [PMID: 12105227]
2.  Kim, H.J., Qiao, Q., Toop, H.D., Morris, J.C. and Don, A.S. A fluorescent assay for ceramide synthase activity. J. Lipid Res. 53 (2012) 1701–1707. [PMID: 22661289]
3.  Wang, Z., Wen, L., Zhu, F., Wang, Y., Xie, Q., Chen, Z. and Li, Y. Overexpression of ceramide synthase 1 increases C18-ceramide and leads to lethal autophagy in human glioma. Oncotarget 8 (2017) 104022–104036. [PMID: 29262618]
4.  Turpin-Nolan, S.M., Hammerschmidt, P., Chen, W., Jais, A., Timper, K., Awazawa, M., Brodesser, S. and Bruning, J.C. CerS1-derived C18:0 ceramide in skeletal muscle promotes obesity-induced insulin resistance. Cell Rep. 26 (2019) 1–10.e7. [PMID: 30605666]
[EC 2.3.1.299 created 2019]
 
 
EC 2.3.2.23     
Accepted name: E2 ubiquitin-conjugating enzyme
Reaction: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Other name(s): ubiquitin-carrier-protein E2; UBC (ambiguous); ubiquitin-conjugating enzyme E2
Systematic name: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
Comments: The E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme (EC 6.2.1.45) and binds it via a transthioesterification reaction to itself. In the human enzyme the catalytic center is located at Cys-87 where ubiquitin is bound via its C-terminal glycine in a thioester linkage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  van Wijk, S.J. and Timmers, H.T. The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J. 24 (2010) 981–993. [DOI] [PMID: 19940261]
2.  David, Y., Ziv, T., Admon, A. and Navon, A. The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J. Biol. Chem. 285 (2010) 8595–8604. [DOI] [PMID: 20061386]
3.  Papaleo, E., Casiraghi, N., Arrigoni, A., Vanoni, M., Coccetti, P. and De Gioia, L. Loop 7 of E2 enzymes: an ancestral conserved functional motif involved in the E2-mediated steps of the ubiquitination cascade. PLoS One 7:e40786 (2012). [DOI] [PMID: 22815819]
4.  Cook, B.W. and Shaw, G.S. Architecture of the catalytic HPN motif is conserved in all E2 conjugating enzymes. Biochem. J. 445 (2012) 167–174. [DOI] [PMID: 22563859]
5.  Li, D.F., Feng, L., Hou, Y.J. and Liu, W. The expression, purification and crystallization of a ubiquitin-conjugating enzyme E2 from Agrocybe aegerita underscore the impact of His-tag location on recombinant protein properties. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 (2013) 153–157. [DOI] [PMID: 23385757]
[EC 2.3.2.23 created 2015]
 
 
EC 2.4.1.1     
Accepted name: glycogen phosphorylase
Reaction: [(1→4)-α-D-glucosyl]n + phosphate = [(1→4)-α-D-glucosyl]n-1 + α-D-glucose 1-phosphate
For diagram of glycogen, click here
Other name(s): muscle phosphorylase a and b; amylophosphorylase; polyphosphorylase; amylopectin phosphorylase; glucan phosphorylase; α-glucan phosphorylase; 1,4-α-glucan phosphorylase; glucosan phosphorylase; granulose phosphorylase; maltodextrin phosphorylase; muscle phosphorylase; myophosphorylase; potato phosphorylase; starch phosphorylase; 1,4-α-D-glucan:phosphate α-D-glucosyltransferase; phosphorylase (ambiguous)
Systematic name: (1→4)-α-D-glucan:phosphate α-D-glucosyltransferase
Comments: This entry covers several enzymes from different sources that act in vivo on different forms of (1→4)-α-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of α-1,4-glucosidic bonds from the non-reducing ends of linear poly(1→4)-α-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an α-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9035-74-9
References:
1.  Hanes, C.S. The breakdown and synthesis of starch by an enzyme from pea seeds. Proc. R. Soc. Lond. B Biol. Sci. 128 (1940) 421–450.
2.  Green, A.A. and Cori, G.T. Crystalline muscle phosphorylase. I. Preparation, properties, and molecular weight. J. Biol. Chem. 151 (1943) 21–29.
3.  Baum, H. and Gilbert, G.A. A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme. Nature 171 (1953) 983–984. [PMID: 13063502]
4.  Cowgill, R.W. Lobster muscle phosphorylase: purfication and properties. J. Biol. Chem. 234 (1959) 3146–3153. [PMID: 13812491]
5.  Chen, G.S. and Segel, I.H. Purification and properties of glycogen phosphorylase from Escherichia coli. Arch. Biochem. Biophys. 127 (1968) 175–186. [DOI] [PMID: 4878695]
6.  Fischer, E.H., Pocker, A. and Saari, J.C. The structure, function and control of glycogen phosphorylase. In: Campbell, P.N. and Greville, G.D. (Ed.), Essays in Biochemistry, vol. 6, Academic Press, London and New York, 1970, pp. 23–68.
[EC 2.4.1.1 created 1961, modified 2013]
 
 
EC 2.4.1.18     
Accepted name: 1,4-α-glucan branching enzyme
Reaction: Transfers a segment of a (1→4)-α-D-glucan chain to a primary hydroxy group in a similar glucan chain
Other name(s): branching enzyme; amylo-(1,4→1,6)-transglycosylase; Q-enzyme; α-glucan-branching glycosyltransferase; amylose isomerase; enzymatic branching factor; branching glycosyltransferase; enzyme Q; glucosan transglycosylase; glycogen branching enzyme; plant branching enzyme; α-1,4-glucan:α-1,4-glucan-6-glycosyltransferase; starch branching enzyme; 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase
Systematic name: (1→4)-α-D-glucan:(1→4)-α-D-glucan 6-α-D-[(1→4)-α-D-glucano]-transferase
Comments: Converts amylose into amylopectin. The accepted name requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme. The latter has frequently been termed Q-enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9001-97-2
References:
1.  Barker, S.A., Bourne, E. and Peat, S. The enzymic synthesis and degradation of starch. Part IV. The purification and storage of the Q-enzyme of the potato. J. Chem. Soc. (Lond.) (1949) 1705–1711.
2.  Baum, H. and Gilbert, G.A. A simple method for the preparation of crystalline potato phosphorylase and Q-enzyme. Nature 171 (1953) 983–984. [PMID: 13063502]
3.  Hehre, E.J. Enzymic synthesis of polysaccharides: a biological type of polymerization. Adv. Enzymol. Relat. Subj. Biochem. 11 (1951) 297–337. [PMID: 24540594]
4.  Illingworth Brown, B. and Brown, D.H. α-1,4-Glucan:α-1,4-glucan 6-glycosyltransferase from mammalian muscle. Methods Enzymol. 8 (1966) 395–403.
[EC 2.4.1.18 created 1961]
 
 
EC 2.4.1.131     
Accepted name: GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase
Reaction: 2 GDP-α-D-mannose + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = 2 GDP + α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): ALG11; ALG11 mannosyltransferase; LEW3 (gene name); At2G40190 (gene name); gmd3 (gene name); galactomannan deficiency protein 3; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase; glycolipid 2-α-mannosyltransferase; GDP-mannose:glycolipid 2-α-D-mannosyltransferase; GDP-Man:Man3GlcNAc2-PP-Dol α-1,2-mannosyltransferase; GDP-α-D-mannose:D-Man-α-(1→3)-[D-Man-α-(1→6)]-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase
Systematic name: GDP-α-D-mannose:α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in α(1→2) linkages to the nascent oligosaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74506-43-7
References:
1.  O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
2.  Absmanner, B., Schmeiser, V., Kampf, M. and Lehle, L. Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an α1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. Biochem. J. 426 (2010) 205–217. [DOI] [PMID: 19929855]
3.  Schutzbach, J.S., Springfield, J.D. and Jensen, J.W. The biosynthesis of oligosaccharide-lipids. Formation of an α-1,2-mannosyl-mannose linkage. J. Biol. Chem. 255 (1980) 4170–4175. [PMID: 6154707]
[EC 2.4.1.131 created 1984, modified 2011, modified 2012]
 
 
EC 2.4.1.132     
Accepted name: GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase
Reaction: GDP-α-D-mannose + β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Glossary: β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = β-D-mannosyl-(1→4)-N,N′-diacetylchitobiosyldiphosphodolichol
Other name(s): Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase
Systematic name: GDP-α-D-mannose:β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 3-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81181-76-2
References:
1.  Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900–11912. [DOI] [PMID: 19282279]
2.  O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
[EC 2.4.1.132 created 1984, modified 2011, modified 2012]
 
 
EC 2.4.1.150     
Accepted name: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-R = UDP + β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-[β-D-GlcNAc-(1→6)]-β-D-Gal-(1→4)-β-D-GlcNAc-R
Glossary: β-D-galactosyl-(1→4)-N-acetyl-D-glucosaminyl-R = type 2 precursor disaccharide
Other name(s): GCNT2 (gene name); GCNT3 (gene name); IGnT; I-branching β1,6-N-acetylglucosaminyltransferase; N-acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-acetyllactosaminide β1→6-acetylglucosaminyltransferase; Galβ1→4GlcNAc-R β1→6 N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide β-1,6-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminide 6-β-N-acetylglucosaminyltransferase (configuration-inverting)
Comments: The enzyme acts on poly-N-acetyllactosamine [glycan chains of β-D-galactosyl-(1→4)-N-acetyl-D-glucosamine units connected by β(1,3) linkages] attached to proteins or lipids. It transfers a GlcNAc residue by β(1,6)-linkage to galactosyl residues close to non-reducing terminals, introducing a branching pattern known as I branching.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85638-40-0
References:
1.  Van den Eijnden, D.H., Winterwerp, H., Smeeman, P. and Schiphorst, W.E.C.M. Novikoff ascites tumor cells contain N-acetyllactosaminide β1→3 and β1→6 N-acetylglucosaminyltransferase activity. J. Biol. Chem. 258 (1983) 3435–3437. [PMID: 6219989]
2.  Basu, M. and Basu, S. Biosynthesis in vitro of Ii core glycosphingolipids from neolactotetraosylceramide by β 1-3- and β 1-6-N-acetylglucosaminyltransferases from mouse T-lymphoma. J. Biol. Chem. 259 (1984) 12557–12562. [PMID: 6238026]
3.  Piller, F., Cartron, J.P., Maranduba, A., Veyrieres, A., Leroy, Y. and Fournet, B. Biosynthesis of blood group I antigens. Identification of a UDP-GlcNAc:GlcNAc β1-3Gal(-R) β1-6(GlcNAc to Gal) N-acetylglucosaminyltransferase in hog gastric mucosa. J. Biol. Chem. 259 (1984) 13385–13390. [PMID: 6490658]
4.  Bierhuizen, M.F., Maemura, K., Kudo, S. and Fukuda, M. Genomic organization of core 2 and I branching β-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the β-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology 5 (1995) 417–425. [DOI] [PMID: 7579796]
5.  Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O., Clausen, H., Fukuda, M.N. and Fukuda, M. Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and β1,4-galactosyltransferase I. J. Biol. Chem. 274 (1999) 9296–9304. [DOI] [PMID: 10092606]
6.  Yeh, J.C., Ong, E. and Fukuda, M. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J. Biol. Chem. 274 (1999) 3215–3221. [DOI] [PMID: 9915862]
[EC 2.4.1.150 created 1984 (EC 2.4.1.164 created 1989, incorporated 2016), modified 2017]
 
 
EC 2.4.1.153     
Accepted name: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + dolichyl phosphate = UDP + dolichyl N-acetyl-α-D-glucosaminyl phosphate
Other name(s): aglK (gene name); dolichyl-phosphate α-N-acetylglucosaminyltransferase; UDP-N-acetyl-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:dolichyl-phosphate α-N-acetyl-D-glucosaminyltransferase
Comments: The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, initiates N-linked glycosylation in that organism. The enzyme differs from the eukaryotic enzyme, which leaves one additional phosphate group on the dolichyl product (cf. EC 2.7.8.15, UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63363-73-5
References:
1.  Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367–373. [DOI] [PMID: 23624439]
[EC 2.4.1.153 created 1984, modified 2015]
 
 
EC 2.4.1.184     
Accepted name: galactolipid galactosyltransferase
Reaction: 2 a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = a 1,2-diacyl-3-O-[β-D-galactosyl-(1→6)-β-D-galactosyl]-sn-glycerol + a 1,2-diacyl-sn-glycerol
For diagram of galactosyl diacylglycerol, click here
Glossary: a 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol = monogalactosyldiacylglycerol
Other name(s): galactolipid-galactolipid galactosyltransferase; galactolipid:galactolipid galactosyltransferase; interlipid galactosyltransferase; GGGT; DGDG synthase (ambiguous); digalactosyldiacylglycerol synthase (ambiguous); 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:mono-3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase; SFR2 (gene name)
Systematic name: 1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol:1,2-diacyl-3-O-(β-D-galactosyl)-sn-glycerol β-D-galactosyltransferase
Comments: The enzyme converts monogalactosyldiacylglycerol to digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol. All residues are connected by β linkages. The activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants, which is performed by EC 2.4.1.46, monogalactosyldiacylglycerol synthase, and EC 2.4.1.241, digalactosyldiacylglycerol synthase. Note that the β,β-digalactosyldiacylglycerol formed by this enzyme is different from the more common α,β-digalactosyldiacylglycerol formed by EC 2.4.1.241. The enzyme provides an important mechanism for the stabilization of the chloroplast membranes during freezing and drought stress.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66676-74-2
References:
1.  Dorne, A.-J., Block, M.A., Joyard, J. and Douce, R. The galactolipid-galactolipid galactosyltransferase is located on the outer surface of the outer-membrane of the chloroplast envelope. FEBS Lett. 145 (1982) 30–34.
2.  Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A., Dorne, A.-J. and Douce, R. Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer envelope membrane of spinach chloroplasts. Biochim. Biophys. Acta 877 (1986) 281–289.
3.  Heemskerk, J.W.M., Jacobs, F.H.H. and Wintermans, J.F.G.M. UDPgalactose-independent synthesis of monogalactosyldiacylglycerol. An enzymatic activity of the spinach chloroplast envelope. Biochim. Biophys. Acta 961 (1988) 38–47. [DOI]
4.  Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694–2706. [DOI] [PMID: 14600212]
5.  Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397–2400. [DOI] [PMID: 15590685]
6.  Fourrier, N., Bedard, J., Lopez-Juez, E., Barbrook, A., Bowyer, J., Jarvis, P., Warren, G. and Thorlby, G. A role for SENSITIVE TO FREEZING2 in protecting chloroplasts against freeze-induced damage in Arabidopsis. Plant J. 55 (2008) 734–745. [DOI] [PMID: 18466306]
7.  Moellering, E.R., Muthan, B. and Benning, C. Freezing tolerance in plants requires lipid remodeling at the outer chloroplast membrane. Science 330 (2010) 226–228. [DOI] [PMID: 20798281]
[EC 2.4.1.184 created 1990, modified 2005, modified 2015]
 
 
EC 2.4.1.229     
Accepted name: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-α-D-glucosaminyl)-trans-4-hydroxy-L-proline
Other name(s): Skp1-HyPro GlcNAc-transferase; UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase; UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase; UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase; UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase
Systematic name: UDP-N-acetyl-α-D-glucosamine:[Skp1-protein]-trans-4-hydroxy-L-proline N-acetyl-α-D-glucosaminyl-transferase
Comments: Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galα1-6Galα1-L-Fucα1-2Galβ1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 256531-81-4
References:
1.  van der Wel, H., Morris, H.R., Panico, M., Paxton, T., Dell, A., Kaplan, L. and West, C.M. Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of Dictyostelium. J. Biol. Chem. 277 (2002) 46328–46337. [DOI] [PMID: 12244115]
2.  Teng-umnuay, P., van der Wel, H. and West, C.M. Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium. J. Biol. Chem. 274 (1999) 36392–36402. [DOI] [PMID: 10593934]
3.  West, C.M., van der Wel, H. and Gaucher, E.A. Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins. Glycobiology 12 (2002) 17. [DOI] [PMID: 11886837]
[EC 2.4.1.229 created 2003, modified 2013]
 
 
EC 2.4.1.242     
Accepted name: NDP-glucose—starch glucosyltransferase
Reaction: NDP-glucose + [(1→4)-α-D-glucosyl]n = NDP + [(1→4)-α-D-glucosyl]n+1
Other name(s): granule-bound starch synthase; starch synthase II (ambiguous); waxy protein; starch granule-bound nucleoside diphosphate glucose-starch glucosyltransferase; granule-bound starch synthase I; GBSSI; granule-bound starch synthase II; GBSSII; GBSS; NDPglucose-starch glucosyltransferase
Systematic name: NDP-glucose:(1→4)-α-D-glucan 4-α-D-glucosyltransferase
Comments: Unlike EC 2.4.1.11, glycogen(starch) synthase and EC 2.4.1.21, starch synthase, which use UDP-glucose and ADP-glucose, respectively, this enzyme can use either UDP- or ADP-glucose. Mutants that lack the Wx (waxy) allele cannot produce this enzyme, which plays an important role in the normal synthesis of amylose. In such mutants, only amylopectin is produced in the endosperm [3] or pollen [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-53-2
References:
1.  Tsai, C.-Y. The function of the waxy locus in starch synthesis in maize endosperm. Biochem. Genet. 11 (1974) 83–96. [PMID: 4824506]
2.  Nakamura, T., Vrinten, P., Hayakawa, K. and Ikeda, J. Characterization of a granule-bound starch synthase isoform found in the pericarp of wheat. Plant Physiol. 118 (1998) 451–459. [PMID: 9765530]
3.  Fujita, N. and Taira, T. A 56-kDa protein is a novel granule-bound starch synthase existing in the pericarps, aleurone layers, and embryos of immature seed in diploid wheat (Triticum monococcum L.). Planta 207 (1998) 125–132. [DOI] [PMID: 9951718]
4.  Murai, J., Taira, T. and Ohta, D. Isolation and characterization of the three Waxy genes encoding the granule-bound starch synthase in hexaploid wheat. Gene 234 (1999) 71–79. [DOI] [PMID: 10393240]
5.  Nelson, O.E. The waxy locus in maize. II The location of the controlling element alleles. Genetics 60 (1968) 507–524. [PMID: 17248421]
[EC 2.4.1.242 created 2005]
 
 
EC 2.4.1.257     
Accepted name: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase
Reaction: GDP-α-D-mannose + α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol = GDP + α-D-Man-(1→3)-[α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
For diagram of dolichyltetradecasaccharide biosynthesis, click here
Other name(s): GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1→3)-D-Man-β-(1→4)-D-GlcNAc-β-(1→4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase
Systematic name: GDP-α-D-mannose:α-D-Man-(1→3)-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol 6-α-D-mannosyltransferase (configuration-retaining)
Comments: The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kampf, M., Absmanner, B., Schwarz, M. and Lehle, L. Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional α1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis. J. Biol. Chem. 284 (2009) 11900–11912. [DOI] [PMID: 19282279]
2.  O'Reilly, M.K., Zhang, G. and Imperiali, B. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. Biochemistry 45 (2006) 9593–9603. [DOI] [PMID: 16878994]
[EC 2.4.1.257 created 2011, modified 2012]
 
 
EC 2.4.1.270     
Accepted name: mannosylglucosyl-3-phosphoglycerate synthase
Reaction: GDP-mannose + 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate = GDP + 2-O-[2-O-(α-D-mannopyranosyl)-α-D-glucopyranosyl]-3-phospho-D-glycerate
Other name(s): MggA
Systematic name: GDP-mannose:2-O-(α-D-glucosyl)-3-phospho-D-glycerate 2-O-α-D-mannosyltransferase
Comments: The enzyme is involved in synthesis of 2-[2-O-(α-D-mannopranosyl)-α-D-glucopyranosyl]-D-glycerate. Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fernandes, C., Mendes, V., Costa, J., Empadinhas, N., Jorge, C., Lamosa, P., Santos, H. and da Costa, M.S. Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis. J. Bacteriol. 192 (2010) 1624–1633. [DOI] [PMID: 20061481]
[EC 2.4.1.270 created 2011]
 
 
EC 2.4.1.277     
Accepted name: 10-deoxymethynolide desosaminyltransferase
Reaction: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose + 10-deoxymethynolide = dTDP + 10-deoxymethymycin
For diagram of methymycin biosynthesis, click here and for diagram of pikromycin biosynthesis, click here
Glossary: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose = dTDP-D-desosamine
Other name(s): glycosyltransferase DesVII; DesVII
Systematic name: dTDP-3-dimethylamino-3,4,6-trideoxy-α-D-glucopyranose:10-deoxymethynolide 3-dimethylamino-4,6-dideoxy-α-D-glucosyltransferase
Comments: DesVII is the glycosyltransferase responsible for the attachment of dTDP-D-desosamine to 10-deoxymethynolide or narbonolide during the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin in the bacterium Streptomyces venezuelae. Activity requires an additional protein partner, DesVIII.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Borisova, S.A. and Liu, H.W. Characterization of glycosyltransferase DesVII and its auxiliary partner protein DesVIII in the methymycin/picromycin biosynthetic pathway. Biochemistry 49 (2010) 8071–8084. [DOI] [PMID: 20695498]
2.  Borisova, S.A., Kim, H.J., Pu, X. and Liu, H.W. Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications. ChemBioChem 9 (2008) 1554–1558. [DOI] [PMID: 18548476]
3.  Hong, J.S., Park, S.J., Parajuli, N., Park, S.R., Koh, H.S., Jung, W.S., Choi, C.Y. and Yoon, Y.J. Functional analysis of DesVIII homologues involved in glycosylation of macrolide antibiotics by interspecies complementation. Gene 386 (2007) 123–130. [DOI] [PMID: 17049185]
[EC 2.4.1.277 created 2011, modified 2014]
 
 
EC 2.4.1.283     
Accepted name: 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
Reaction: UDP-N-acetyl-α-D-glucosamine + 2-deoxystreptamine = UDP + 2′-N-acetylparomamine
For diagram of paromamine biosynthesis, click here
Other name(s): btrM (gene name); neoD (gene name); kanF (gene name)
Systematic name: UDP-N-acetyl-α-D-glucosamine:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Unlike the enzyme from the bacterium Streptomyces kanamyceticus, which can also accept UDP-D-glucose [2] (cf. EC 2.4.1.284, 2-deoxystreptamine glucosyltransferase), the enzyme from Bacillus circulans can only accept UDP-N-acetyl-α-D-glucosamine [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744]
2.  Park, J.W., Park, S.R., Nepal, K.K., Han, A.R., Ban, Y.H., Yoo, Y.J., Kim, E.J., Kim, E.M., Kim, D., Sohng, J.K. and Yoon, Y.J. Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic manipulation. Nat. Chem. Biol. 7 (2011) 843–852. [DOI] [PMID: 21983602]
[EC 2.4.1.283 created 2012]
 
 
EC 2.4.1.290     
Accepted name: N,N′-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglA
Systematic name: UDP-N-acetyl-α-D-galactosamine:N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase
Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
[EC 2.4.1.290 created 2012]
 
 
EC 2.4.1.291     
Accepted name: N-acetylgalactosamine-N,N′-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→4)-N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglJ
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetylgalactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase
Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
2.  Chen, M.M., Weerapana, E., Ciepichal, E., Stupak, J., Reid, C.W., Swiezewska, E. and Imperiali, B. Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 46 (2007) 14342–14348. [DOI] [PMID: 18034500]
[EC 2.4.1.291 created 2012]
 
 
EC 2.4.1.292     
Accepted name: GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase
Reaction: 3 UDP-N-acetyl-α-D-galactosamine + GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol = 3 UDP + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: diNAcBac = N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglH
Systematic name: UDP-N-acetyl-α-D-galactosamine:GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-α-N-acetyl-D-galactosaminyltransferase
Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
2.  Troutman, J.M. and Imperiali, B. Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions. Biochemistry 48 (2009) 2807–2816. [DOI] [PMID: 19159314]
3.  Borud, B., Viburiene, R., Hartley, M.D., Paulsen, B.S., Egge-Jacobsen, W., Imperiali, B. and Koomey, M. Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system. Proc. Natl. Acad. Sci. USA 108 (2011) 9643–9648. [DOI] [PMID: 21606362]
[EC 2.4.1.292 created 2012]
 
 
EC 2.4.1.293     
Accepted name: GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase
Reaction: UDP-α-D-glucose + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol = UDP + [GalNAc-α-(1→4)]2-[Glc-β-(1→3)]-[GalNAc-α-(1→4)]2-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: diNAcBac = N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglI
Systematic name: UDP-α-D-glucose:[GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol 3-β-D-glucosyltransferase
Comments: Isolated from the bacterium Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
2.  Kelly, J., Jarrell, H., Millar, L., Tessier, L., Fiori, L.M., Lau, P.C., Allan, B. and Szymanski, C.M. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J. Bacteriol. 188 (2006) 2427–2434. [DOI] [PMID: 16547029]
[EC 2.4.1.293 created 2012]
 
 
EC 2.4.1.302     
Accepted name: L-demethylnoviosyl transferase
Reaction: dTDP-4-O-demethyl-β-L-noviose + novobiocic acid = dTDP + demethyldecarbamoyl novobiocin
For diagram of novobiocin biosynthesis, click here
Glossary: novobiocic acid = N-(2,7-dihydroxy-8-methyl-4-oxo-4H-chromen-3-yl)-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide
dTDP-4-O-demethyl-β-L-noviose = dTDP-6-deoxy-5-methyl-β-L-altropyranose = dTDP-(2S,3R,4R,5R)-6,6-dimethyltetrahydro-2H-pyran-2,3,4,5-tetraol
demethyldecarbamoyl novobiocin = N-{7-[(6-deoxy-5-methyl-β-D-gulopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-chromen-3-yl}-4-hydroxy-3-(3-methylbut-2-en-1-yl)benzamide
Other name(s): novM (gene name); dTDP-β-L-noviose:novobiocic acid 7-O-noviosyltransferase; L-noviosyl transferase
Systematic name: dTDP-4-O-demethyl-β-L-noviose:novobiocic acid 7-O-[4-O-demethyl-L-noviosyl]transferase
Comments: The enzyme is involved in the biosynthesis of the aminocoumarin antibiotic, novobiocin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Freel Meyers, C.L., Oberthur, M., Anderson, J.W., Kahne, D. and Walsh, C.T. Initial characterization of novobiocic acid noviosyl transferase activity of NovM in biosynthesis of the antibiotic novobiocin. Biochemistry 42 (2003) 4179–4189. [DOI] [PMID: 12680772]
2.  Albermann, C., Soriano, A., Jiang, J., Vollmer, H., Biggins, J.B., Barton, W.A., Lesniak, J., Nikolov, D.B. and Thorson, J.S. Substrate specificity of NovM: implications for novobiocin biosynthesis and glycorandomization. Org. Lett. 5 (2003) 933–936. [DOI] [PMID: 12633109]
[EC 2.4.1.302 created 2013, modified 2016]
 
 
EC 2.4.1.335     
Accepted name: dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase
Reaction: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate + an archaeal dolichyl N-acetyl-α-D-glucosaminyl phosphate = UDP + an archaeal dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-β-D-glucuronsyl)-N-acetyl-α-D-glucosaminyl phosphate
Other name(s): AglC; UDP-Glc-2,3-diNAcA glycosyltransferase
Systematic name: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate:dolichyl N-acetyl-α-D-glucosaminyl-phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase
Comments: The enzyme, characterized from the methanogenic archaeon Methanococcus voltae, participates in the N-glycosylation of proteins. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367–373. [DOI] [PMID: 23624439]
[EC 2.4.1.335 created 2015]
 
 
EC 2.4.1.370     
Accepted name: inositol phosphorylceramide mannosyltransferase
Reaction: GDP-α-D-mannose + a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine + GDP
Glossary: a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine = a very-long-chain inositol phospho-α hydroxyphytoceramide = IPC
a (4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-{[6-O-(α-D-mannosyl)-1D-myo-inositol-1-O-yl]hydroxyphosphoryl}sphinganine = a very-long-chain mannosylinositol phospho-α-hydroxyphytoceramide = MIPC
Other name(s): SUR1 (gene name); CSH1 (gene name)
Systematic name: GDP-α-D-mannose:(4R)-4-hydroxy-N-[(2R)-2-hydroxy-very-long-chain-acyl]-1-O-[(1D-myo-inositol-1-O-yl)hydroxyphosphoryl]sphinganine mannosyltransferase (configuration-retaining)
Comments: The simplest complex sphingolipid of yeast, inositol-phospho-α-hydroxyphytoceramide (IPC), is usually mannosylated to yield mannosyl-inositol-phospho-α hydroxyphytoceramide (MIPC). The enzyme is located in the Golgi apparatus, and utilizes GDP-mannose as the mannosyl group donor. It consists of a catalytic subunit (SUR1 or CSH1) and a regulatory subunit (CSG2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Beeler, T.J., Fu, D., Rivera, J., Monaghan, E., Gable, K. and Dunn, T.M. SUR1 (CSG1/BCL21), a gene necessary for growth of Saccharomyces cerevisiae in the presence of high Ca2+ concentrations at 37 degrees C, is required for mannosylation of inositolphosphorylceramide. Mol. Gen. Genet. 255 (1997) 570–579. [DOI] [PMID: 9323360]
2.  Dean, N., Zhang, Y.B. and Poster, J.B. The VRG4 gene is required for GDP-mannose transport into the lumen of the Golgi in the yeast, Saccharomyces cerevisiae. J. Biol. Chem. 272 (1997) 31908–31914. [DOI] [PMID: 9395539]
3.  Uemura, S., Kihara, A., Inokuchi, J. and Igarashi, Y. Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p. J. Biol. Chem. 278 (2003) 45049–45055. [DOI] [PMID: 12954640]
[EC 2.4.1.370 created 2019]
 
 
EC 2.4.1.372     
Accepted name: mutansucrase
Reaction: sucrose + [(1→3)-α-D-glucosyl]n = D-fructose + [(1→3)-α-D-glucosyl]n+1
Other name(s): gtfJ (gene name)
Systematic name: sucrose:(1→3)-α-D-glucan 3-α-D-glucosyltransferase
Comments: The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. This enzyme extends the glucan chain by an α(1→3) linkage.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Simpson, C.L., Cheetham, N.W., Giffard, P.M. and Jacques, N.A. Four glucosyltransferases, GtfJ, GtfK, GtfL and GtfM, from Streptococcus salivarius ATCC 25975. Microbiology 141 (1995) 1451–1460. [PMID: 7545511]
2.  Puanglek, S., Kimura, S., Enomoto-Rogers, Y., Kabe, T., Yoshida, M., Wada, M. and Iwata, T. In vitro synthesis of linear α-1,3-glucan and chemical modification to ester derivatives exhibiting outstanding thermal properties. Sci. Rep. 6:30479 (2016). [PMID: 27469976]
[EC 2.4.1.372 created 2019]
 
 
EC 2.4.1.383     
Accepted name: GDP-Man:α-L-Rha-(1→3)-α-D-Gal-PP-Und β-1,4-mannosyltransferase
Reaction: GDP-α-D-mannose + α-L-Rha-(1→3)-α-D-Gal-PP-Und = GDP + β-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und
Glossary: α-L-Rha-(1→3)-α-D-Gal-PP-Und = α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
β-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und = β-D-mannopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): wbaO (gene name); rfbO (gene name)
Systematic name: GDP-α-D-mannose:α-L-rhamnopyranosyl-(1→3)-α-D-galactopyranosyl-diphospho-ditrans,octacis-undecaprenol 4II-β-mannosyltransferase (configuration inverting)
Comments: The enzyme participates in the biosynthesis of the O antigens produced by group E and D2 strains of the pathogenic bacterium Salmonella enterica.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xiang, S.H., Hobbs, M. and Reeves, P.R. Molecular analysis of the rfb gene cluster of a group D2 Salmonella enterica strain: evidence for its origin from an insertion sequence-mediated recombination event between group E and D1 strains. J. Bacteriol. 176 (1994) 4357–4365. [DOI] [PMID: 8021222]
2.  Zhao, Y., Biggins, J. B. and Thorson, J. S. Acceptor specificity of Salmonella GDP-Man:α-L-Rha-(1→3)-α-D- Gal- PP-Und β(1→4)-mannosyltransferase: A simplified assay based on unnatural acceptors. J. Am. Chem. Soc. 120 (1998) 12986–12987. [DOI]
3.  Zhao, Y. and Thorson, J.S. Chemoenzymatic synthesis of the Salmonella group E1 core trisaccharide using a recombinant β-(1-→4)-mannosyltransferase. Carbohydr. Res. 319 (1999) 184–191. [DOI] [PMID: 10520265]
[EC 2.4.1.383 created 2021]
 
 
EC 2.4.1.392     
Accepted name: 3-O-β-D-glucopyranosyl-β-D-glucuronide phosphorylase
Reaction: a 3-O-β-D-glucosyl-β-D-glucuronoside + phosphate = a β-D-glucuronoside + α-D-glucopyranose 1-phosphate
Other name(s): PBOR_13355 (locus name)
Systematic name: 3-O-β-D-glucopyranosyl-β-D-glucuronide:phosphate α-D-glucosyltransferase
Comments: The enzyme, characterized from the bacterium Paenibacillus borealis, catalyses a reversible reaction, transferring a glucosyl residue attached by a β(1,3) linkage to a D-glucuronate residue (either free or as a part of a β-D-glucuronide) to a free phosphate, generating α-D-glucopyranose 1-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Isono, N., Mizutani, E., Hayashida, H., Katsuzaki, H. and Saburi, W. Functional characterization of a novel GH94 glycoside phosphorylase, 3-O-β-D-glucopyranosyl β-D-glucuronide phosphorylase, and implication of the metabolic pathway of acidic carbohydrates in Paenibacillus borealis. Biochem. Biophys. Res. Commun. 625 (2022) 60–65. [DOI] [PMID: 35947916]
[EC 2.4.1.392 created 2022]
 
 
EC 2.4.2.8     
Accepted name: hypoxanthine phosphoribosyltransferase
Reaction: IMP + diphosphate = hypoxanthine + 5-phospho-α-D-ribose 1-diphosphate
Other name(s): IMP pyrophosphorylase; transphosphoribosidase; hypoxanthine—guanine phosphoribosyltransferase; guanine phosphoribosyltransferase; GPRT; HPRT; guanosine 5′-phosphate pyrophosphorylase; IMP-GMP pyrophosphorylase; HGPRTase; 6-hydroxypurine phosphoribosyltransferase; 6-mercaptopurine phosphoribosyltransferase; GMP pyrophosphorylase; guanine-hypoxanthine phosphoribosyltransferase; guanosine phosphoribosyltransferase; guanylate pyrophosphorylase; guanylic pyrophosphorylase; inosinate pyrophosphorylase; inosine 5′-phosphate pyrophosphorylase; inosinic acid pyrophosphorylase; inosinic pyrophosphorylase; purine-6-thiol phosphoribosyltransferase
Systematic name: IMP:diphosphate phospho-D-ribosyltransferase
Comments: Guanine and purine-6-thiol can replace hypoxanthine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9016-12-0
References:
1.  Flaks, J.G. Nucleotide synthesis from 5-phosphoribosylpyrophosphate. Methods Enzymol. 6 (1963) 136–158.
2.  Kornberg, A., Lieberman, I. and Simms, E.S. Enzymatic synthesis of purine nucleotides. J. Biol. Chem. 215 (1955) 417–427. [PMID: 14392175]
3.  Lukens, L.N. and Herrington, K.A. Enzymic formation of 6-mercaptopurine ribotide. Biochim. Biophys. Acta 24 (1957) 432–433. [PMID: 13436452]
4.  Remy, C.N., Remy, W.T. and Buchanan, J.M. Biosynthesis of the purines. VIII. Enzymatic synthesis and utilization of α-5-phosphoribosylpyrophosphate. J. Biol. Chem. 217 (1955) 885–895. [PMID: 13271449]
[EC 2.4.2.8 created 1961, modified 1982]
 
 
EC 2.4.2.43     
Accepted name: lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
Reaction: (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-α-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate
For diagram of lipid IIA biosynthesis, click here
Glossary: lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4′-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
Other name(s): undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK; arnT (gene name)
Systematic name: 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl-phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase
Comments: Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122–43131. [DOI] [PMID: 11535604]
2.  Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132–43144. [DOI] [PMID: 11535605]
3.  Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111–43121. [DOI] [PMID: 11535603]
4.  Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33–39. [DOI] [PMID: 16226890]
5.  Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29–35. [DOI] [PMID: 19947657]
[EC 2.4.2.43 created 2010, modified 2011]
 
 
EC 2.4.2.49     
Accepted name: neamine phosphoribosyltransferase
Reaction: neamine + 5-phospho-α-D-ribose 1-diphosphate = 5′′-phosphoribostamycin + diphosphate
For diagram of neamine and ribostamycin biosynthesis, click here
Glossary: neamine = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl]oxy}oxane-3,4-diol
ribostamycin = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol
Other name(s): btrL (gene name); neoM (gene name)
Systematic name: neamine:5-phospho-α-D-ribose 1-diphosphate phosphoribosyltransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. The enzyme requires a divalent metal ion, optimally Mg2+, Ni2+ or Co2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360–4368. [DOI] [PMID: 17482823]
[EC 2.4.2.49 created 2013]
 
 
EC 2.4.99.17     
Accepted name: S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Reaction: S-adenosyl-L-methionine + 7-aminomethyl-7-carbaguanosine34 in tRNA = L-methionine + adenine + epoxyqueuosine34 in tRNA
For diagram of queuine biosynthesis, click here
Glossary: 7-aminomethyl-7-carbaguanine = preQ1 = 7-aminomethyl-7-deazaguanine
epoxyqueosine = oQ
Other name(s): QueA enzyme; queuosine biosynthesis protein QueA
Systematic name: S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing)
Comments: The reaction is a combined transfer and isomerization of the ribose moiety of S-adenosyl-L-methionine to the modified guanosine base in the wobble position in tRNAs specific for Tyr, His, Asp or Asn. It is part of the queuosine biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Slany, R.K., Bosl, M., Crain, P.F. and Kersten, H. A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine. Biochemistry 32 (1993) 7811–7817. [PMID: 8347586]
2.  Slany, R.K., Bosl, M. and Kersten, H. Transfer and isomerization of the ribose moiety of AdoMet during the biosynthesis of queuosine tRNAs, a new unique reaction catalyzed by the QueA protein from Escherichia coli. Biochimie 76 (1994) 389–393. [DOI] [PMID: 7849103]
3.  Kinzie, S.D., Thern, B. and Iwata-Reuyl, D. Mechanistic studies of the tRNA-modifying enzyme QueA: a chemical imperative for the use of AdoMet as a "ribosyl" donor. Org. Lett. 2 (2000) 1307–1310. [PMID: 10810734]
4.  Van Lanen, S.G. and Iwata-Reuyl, D. Kinetic mechanism of the tRNA-modifying enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA). Biochemistry 42 (2003) 5312–5320. [DOI] [PMID: 12731872]
5.  Mathews, I., Schwarzenbacher, R., McMullan, D., Abdubek, P., Ambing, E., Axelrod, H., Biorac, T., Canaves, J.M., Chiu, H.J., Deacon, A.M., DiDonato, M., Elsliger, M.A., Godzik, A., Grittini, C., Grzechnik, S.K., Hale, J., Hampton, E., Han, G.W., Haugen, J., Hornsby, M., Jaroszewski, L., Klock, H.E., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., Levin, I., Miller, M.D., Moy, K., Nigoghossian, E., Ouyang, J., Paulsen, J., Quijano, K., Reyes, R., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., Vincent, J., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J. and Wilson, I.A. Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 Å resolution reveals a new fold. Proteins 59 (2005) 869–874. [DOI] [PMID: 15822125]
6.  Grimm, C., Ficner, R., Sgraja, T., Haebel, P., Klebe, G. and Reuter, K. Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase. Biochem. Biophys. Res. Commun. 351 (2006) 695–701. [DOI] [PMID: 17083917]
[EC 2.4.99.17 created 2012]
 
 
EC 2.4.99.21     
Accepted name: dolichyl-phosphooligosaccharide-protein glycotransferase
Reaction: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-β-D-glycosyl linkage to a protein L-asparagine
Other name(s): AglB; archaeal oligosaccharyl transferase; dolichyl-monophosphooligosaccharide-protein glycotransferase
Systematic name: dolichyl-phosphooligosaccharide:protein-L-asparagine N-β-D-oligosaccharidotransferase
Comments: The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins. It is different from EC 2.4.99.18, dolichyl-diphosphooligosaccharide-protein glycotransferase, which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes. The enzyme participates in the N-glycosylation of proteins in some archaea. It requires Mn2+. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is α,ω-saturated and it may have additional unsaturated positions in the chain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Chaban, B., Voisin, S., Kelly, J., Logan, S.M. and Jarrell, K.F. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea. Mol. Microbiol. 61 (2006) 259–268. [DOI] [PMID: 16824110]
2.  Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nat. Chem. Biol. 9 (2013) 367–373. [DOI] [PMID: 23624439]
3.  Cohen-Rosenzweig, C., Guan, Z., Shaanan, B. and Eichler, J. Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans. Appl. Environ. Microbiol. 80 (2014) 486–496. [DOI] [PMID: 24212570]
[EC 2.4.99.21 created 2015]
 
 
EC 2.5.1.18     
Accepted name: glutathione transferase
Reaction: RX + glutathione = HX + R-S-glutathione
Other name(s): glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST
Systematic name: RX:glutathione R-transferase
Comments: A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50812-37-8
References:
1.  Habig, W.H., Pabst, M.J. and Jakoby, W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130–7139. [PMID: 4436300]
2.  Jakoby, W.B. The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 46 (1978) 383. [PMID: 345769]
3.  Jakoby, W.B. Glutathione transferases: an overview. Methods Enzymol. 113 (1985) 495–499. [PMID: 4088070]
4.  Keen, J.H. and Jakoby, W.B. Glutathione transferases. Catalysis of nucleophilic reactions of glutathione. J. Biol. Chem. 253 (1978) 5654–5657. [PMID: 670218]
5.  Sheehan, D., Meade, G., Foley, V.M. and Dowd, C.A. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1–16. [PMID: 11695986]
[EC 2.5.1.18 created 1976 (EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7 created 1972, incorporated 1976)]
 
 
EC 2.5.1.66     
Accepted name: N2-(2-carboxyethyl)arginine synthase
Reaction: D-glyceraldehyde 3-phosphate + L-arginine = N2-(2-carboxyethyl)-L-arginine + phosphate
For diagram of clavulanate biosynthesis, click here
Other name(s): CEAS; N2-(2-carboxyethyl)arginine synthetase; CEA synthetase; glyceraldehyde-3-phosphate:L-arginine 2-N-(2-hydroxy-3-oxopropyl) transferase (2-carboxyethyl-forming)
Systematic name: glyceraldehyde-3-phosphate:L-arginine N2-(2-hydroxy-3-oxopropyl) transferase (2-carboxyethyl-forming)
Comments: The enzyme requires thiamine diphosphate and catalyses the first step in the clavulanic-acid-biosynthesis pathway. The 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 250207-48-8
References:
1.  Caines, M.E.C., Elkins, J.M., Hewitson, K.S. and Schofield, C.J. Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzymes in the clavulanic acid biosynthesis pathway. J. Biol. Chem. 279 (2004) 5685–5692. [DOI] [PMID: 14623876]
2.  Khaleeli, N., Li, R. and Townsend, C.A. Origin of the β-lactam carbons in clavulanic acid from an unusual thiamine pyrophosphate-mediated reaction. J. Am. Chem. Soc. 121 (1999) 9223–9224.
[EC 2.5.1.66 created 2004]
 
 
EC 2.5.1.87     
Accepted name: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10–55)
For diagram of di- and tritrans,polycis-polyprenol biosynthesis, click here
Other name(s): RER2; Rer2p; Rer2p Z-prenyltransferase; Srt1p; Srt2p Z-prenyltransferase; ACPT; dehydrodolichyl diphosphate synthase 1
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10–55 isopentenyl units)
Comments: The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated α-isoprene unit, which serves as a glycosyl carrier in protein glycosylation [1]. The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13–18 isoprene residues with dominating C80 (16 isoprene residues) extending to C120, while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C290 [2]. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C120 [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sato, M., Fujisaki, S., Sato, K., Nishimura, Y. and Nakano, A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6 (2001) 495–506. [DOI] [PMID: 11442630]
2.  Poznanski, J. and Szkopinska, A. Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Biopolymers 86 (2007) 155–164. [DOI] [PMID: 17345630]
3.  Sato, M., Sato, K., Nishikawa, S., Hirata, A., Kato, J. and Nakano, A. The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell Biol. 19 (1999) 471–483. [DOI] [PMID: 9858571]
4.  Oh, S.K., Han, K.H., Ryu, S.B. and Kang, H. Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis. J. Biol. Chem. 275 (2000) 18482–18488. [DOI] [PMID: 10764783]
5.  Cunillera, N., Arro, M., Fores, O., Manzano, D. and Ferrer, A. Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477 (2000) 170–174. [DOI] [PMID: 10908715]
[EC 2.5.1.87 created 2010]
 
 
EC 2.5.1.144     
Accepted name: S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent)
Reaction: O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate
For diagram of O3-Acetyl-L-serine metabolism, click here
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): cysteine synthase B; cysM (gene name); CS26 (gene name)
Systematic name: O-acetyl-L-serine:thiosulfate 2-amino-2-carboxyethyltransferase
Comments: In plants, the activity is catalysed by a chloroplastic enzyme that plays an important role in chloroplast function and is essential for light-dependent redox regulation within the chloroplast. The bacterial enzyme also catalyses the activity of EC 2.5.1.47, cysteine synthase. cf. EC 2.8.5.1, S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hensel, G. and Truper, H.G. O-Acetylserine sulfhydrylase and S-sulfocysteine synthase activities of Rhodospirillum tenue. Arch. Microbiol. 134 (1983) 227–232. [PMID: 6615127]
2.  Nakamura, T., Iwahashi, H. and Eguchi, Y. Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium. J. Bacteriol. 158 (1984) 1122–1127. [PMID: 6373737]
3.  Bermudez, M.A., Paez-Ochoa, M.A., Gotor, C. and Romero, L.C. Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast function and long-day light-dependent redox control. Plant Cell 22 (2010) 403–416. [DOI] [PMID: 20179139]
4.  Bermudez, M.A., Galmes, J., Moreno, I., Mullineaux, P.M., Gotor, C. and Romero, L.C. Photosynthetic adaptation to length of day is dependent on S-sulfocysteine synthase activity in the thylakoid lumen. Plant Physiol. 160 (2012) 274–288. [DOI] [PMID: 22829322]
5.  Gotor, C. and Romero, L.C. S-Sulfocysteine synthase function in sensing chloroplast redox status. Plant Signal. Behav. 8:e23313 (2013). [DOI] [PMID: 23333972]
[EC 2.5.1.144 created 2018]
 
 
EC 2.6.1.34     
Accepted name: UDP-N-acetylbacillosamine transaminase
Reaction: UDP-N-acetylbacillosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-α-D-xylo-hex-4-ulose + L-glutamate
For diagram of legionaminic acid biosynthesis, click here
Glossary: UDP-N-acetylbacillosamine = UDP-2-acetamido-4-amino-2,4,6-trideoxy-α-D-glucose = UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine
Other name(s): uridine diphospho-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase; UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine transaminase; UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase; pglE (gene name); UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose:2-oxoglutarate aminotransferase
Systematic name: UDP-4-amino-4,6-dideoxy-N-acetyl-α-D-glucosamine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme is involved in biosynthesis of UDP-N,N′-diacetylbacillosamine, an intermediate in protein glycosylation pathways in several bacterial species, including N-linked glycosylation of certain L-asparagine residues in Campylobacter species [2-4] and O-linked glycosylation of certain L-serine residues in Neisseria species [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-89-7
References:
1.  Distler, J., Kaufman, B. and Roseman, S. Enzymic synthesis of a diamino sugar nucleotide by extracts of type XIV Diplococcus pneumoniae. Arch. Biochem. Biophys. 116 (1966) 466–478. [DOI] [PMID: 4381351]
2.  Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. In vitro biosynthesis of UDP-N,N′-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry 45 (2006) 13659–13669. [DOI] [PMID: 17087520]
3.  Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 281 (2006) 723–732. [DOI] [PMID: 16286454]
4.  Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and Young, N.M. Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry 47 (2008) 1827–1836. [DOI] [PMID: 18198901]
5.  Hartley, M.D., Morrison, M.J., Aas, F.E., Borud, B., Koomey, M. and Imperiali, B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N′-diacetylbacillosamine. Biochemistry 50 (2011) 4936–4948. [DOI] [PMID: 21542610]
[EC 2.6.1.34 created 1972, modified 2013]
 
 
EC 2.6.1.52     
Accepted name: phosphoserine transaminase
Reaction: (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + L-glutamate
(2) 4-phosphooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
For diagram of EC 2.6.1, click here, for diagram of serine biosynthesis, click here and for diagram of pyridoxal biosynthesis, click here
Other name(s): PSAT; phosphoserine aminotransferase; 3-phosphoserine aminotransferase; hydroxypyruvic phosphate-glutamic transaminase; L-phosphoserine aminotransferase; phosphohydroxypyruvate transaminase; phosphohydroxypyruvic-glutamic transaminase; 3-O-phospho-L-serine:2-oxoglutarate aminotransferase; SerC; PdxC; 3PHP transaminase
Systematic name: O-phospho-L-serine:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5′-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5′-phosphate biosynthesis in the bacterium Escherichia coli [3]. Pyridoxal 5′-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4]. The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine [7].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-90-4
References:
1.  Pizer, L.I. The pathway and control of serine biosynthesis in Escherichia coli. J. Biol. Chem. 238 (1963) 3934–3944. [PMID: 14086727]
2.  Hirsch, H. and Greenberg, D.M. Studies on phosphoserine aminotransferase of sheep brain. J. Biol. Chem. 242 (1967) 2283–2287. [PMID: 6022873]
3.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [DOI] [PMID: 8550422]
4.  Drewke, C., Klein, M., Clade, D., Arenz, A., Müller, R. and Leistner, E. 4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis. FEBS Lett. 390 (1996) 179–182. [DOI] [PMID: 8706854]
5.  Zhao, G. and Winkler, M.E. 4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5′-phosphate coenzyme biosynthesis in Escherichia coli K-12. FEMS Microbiol. Lett. 135 (1996) 275–280. [PMID: 8595869]
6.  Baek, J.Y., Jun, D.Y., Taub, D. and Kim, Y.H. Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis. Biochem. J. 373 (2003) 191–200. [PMID: 12633500]
7.  Helgadottir, S., Rosas-Sandoval, G., Soll, D. and Graham, D.E. Biosynthesis of phosphoserine in the Methanococcales. J. Bacteriol. 189 (2007) 575–582. [PMID: 17071763]
[EC 2.6.1.52 created 1972, modified 2006]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald