ExplorEnz: EC 2.4.1.3*

Displaying entries 1-50 of 109.

<< Previous | Next >> Printable version

2.4.1.3

Deleted entry:

amylomaltase. Now included with EC 2.4.1.25, 4-α-glucanotransferase

[EC 2.4.1.3 created 1961, deleted 1972]

2.4.1.30

Accepted name:

1,3-β-oligoglucan phosphorylase

Reaction:

[(1→3)-β-D-glucosyl]_n + phosphate = [(1→3)-β-D-glucosyl]_n-1 + α-D-glucose 1-phosphate

Other name(s):

β-1,3-oligoglucan:orthophosphate glucosyltransferase II; β-1,3-oligoglucan phosphorylase; 1,3-β-D-oligoglucan:phosphate α-D-glucosyltransferase

Systematic name:

(1→3)-β-D-glucan:phosphate α-D-glucosyltransferase

Comments:

Does not act on laminarin. Differs in specificity from EC 2.4.1.31 (laminaribiose phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-28-6

References:

1.	Maréchal, L.R. β-1,3-Oligoglucan:orthophosphate glucosyltransferases from Euglena gracilis. I. Isolation and some properties of a β-1,3-oligoglucan phosphorylase. Biochim. Biophys. Acta 146 (1967) 417–430. [DOI] [PMID: 6066291]
2.	Maréchal, L.R. β-1,3-Oligoglucan: orthophosphate glucosyltransferases from Euglena gracilis. II. Comparative studies between laminaribiose- and β-1,3-oligoglucan phosphorylase. Biochim. Biophys. Acta 146 (1967) 431–442. [DOI] [PMID: 6066292]

[EC 2.4.1.30 created 1972]

2.4.1.31

Accepted name:

laminaribiose phosphorylase

Reaction:

3-β-D-glucosyl-D-glucose + phosphate = D-glucose + α-D-glucose 1-phosphate

Systematic name:

3-β-D-glucosyl-D-glucose:phosphate α-D-glucosyltransferase

Comments:

Also acts on 1,3-β-D-oligoglucans. Differs in specificity from EC 2.4.1.30 (1,3-β-oligoglucan phosphorylase) and EC 2.4.1.97 (1,3-β-D-glucan phosphorylase).

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-29-7

References:

1.	Goldemberg, S.H., Maréchal, L.R. and De Souza, B.C. β-1,3-Oligoglucan: orthophosphate glucosyltransferase from Euglena gracilis. J. Biol. Chem. 241 (1966) 45–50. [PMID: 5901055]
2.	Manners, D.J. and Taylor, D.C. Studies on carbohydrate metabolizing enzymes. XVI. Specificity of laminaribiose phosphorylase from Astasia ocellata. Arch. Biochem. Biophys. 121 (1967) 443–451. [DOI] [PMID: 6057111]

[EC 2.4.1.31 created 1972]

2.4.1.32

Accepted name:

glucomannan 4-β-mannosyltransferase

Reaction:

GDP-mannose + (glucomannan)_n = GDP + (glucomannan)_n+1

Other name(s):

GDP-man-β-mannan manosyltransferase; glucomannan-synthase; GDPmannose:glucomannan 1,4-β-D-mannosyltransferase; GDP-mannose:glucomannan 1,4-β-D-mannosyltransferase

Systematic name:

GDP-mannose:glucomannan 4-β-D-mannosyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-30-0

References:

1.	Elbein, A.D. Biosynthesis of a cell wall glucomannan in mung bean seedlings. J. Biol. Chem. 244 (1969) 1608–1616. [PMID: 4304230]

[EC 2.4.1.32 created 1972]

2.4.1.33

Accepted name:

mannuronan synthase

Reaction:

GDP-α-D-mannuronate + [(1→4)-β-D-mannuronosyl]_n = GDP + [(1→4)-β-D-mannuronosyl]_n+1

Glossary:

poly[β-(1,4)-D-mannuronate] = mannuronan

Other name(s):

mannuronosyl transferase; alginate synthase (incorrect); alg8 (gene name); alg44 (gene name); GDP-D-mannuronate:alginate D-mannuronyltransferase

Systematic name:

GDP-α-D-mannuronate:mannuronan D-mannuronatetransferase

Comments:

The enzyme catalyses the polymerization of β-D-mannuronate residues into a mannuronan polymer, an intermediate in the biosynthesis of alginate. It is found in brown algae and in alginate-producing bacterial species from the Pseudomonas and Azotobacter genera.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37257-31-1

References:

1.	Lin, T.-Y. and Hassid, W.Z. Pathway of alginic acid synthesis in the marine brown alga, Fucus gardneri Silva. J. Biol. Chem. 241 (1966) 5284–5297. [PMID: 5954796]
2.	Remminghorst, U. and Rehm, B.H. In vitro alginate polymerization and the functional role of Alg8 in alginate production by Pseudomonas aeruginosa. Appl. Environ. Microbiol. 72 (2006) 298–305. [DOI] [PMID: 16391057]
3.	Oglesby, L.L., Jain, S. and Ohman, D.E. Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization. Microbiology 154 (2008) 1605–1615. [DOI] [PMID: 18524915]

[EC 2.4.1.33 created 1972, modified 2015]

2.4.1.34

Accepted name:

1,3-β-glucan synthase

Reaction:

UDP-glucose + [(1→3)-β-D-glucosyl]_n = UDP + [(1→3)-β-D-glucosyl]_n+1

Other name(s):

1,3-β-D-glucan—UDP glucosyltransferase; UDP-glucose—1,3-β-D-glucan glucosyltransferase; callose synthetase; 1,3-β-D-glucan-UDP glucosyltransferase; UDP-glucose-1,3-β-D-glucan glucosyltransferase; paramylon synthetase; UDP-glucose-β-glucan glucosyltransferase; GS-II; (1,3)-β-glucan (callose) synthase; β-1,3-glucan synthase; β-1,3-glucan synthetase; 1,3-β-D-glucan synthetase; 1,3-β-D-glucan synthase; 1,3-β-glucan-uridine diphosphoglucosyltransferase; callose synthase; UDP-glucose-1,3-β-glucan glucosyltransferase; UDP-glucose:(1,3)β-glucan synthase; uridine diphosphoglucose-1,3-β-glucan glucosyltransferase; UDP-glucose:1,3-β-D-glucan 3-β-D-glucosyltransferase

Systematic name:

UDP-glucose:(1→3)-β-D-glucan 3-β-D-glucosyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-30-3

References:

1.	Maréchal, L.R. and Goldemberg, S.H. Uridine diphosphate glucose-β-1,3-glucan β-3-glucosyltransferase from Euglena gracilis. J. Biol. Chem. 239 (1964) 3163–3167. [PMID: 14245356]

[EC 2.4.1.34 created 1972]

2.4.1.35

Accepted name:

phenol β-glucosyltransferase

Reaction:

UDP-glucose + a phenol = UDP + an aryl β-D-glucoside

Other name(s):

UDPglucosyltransferase (ambiguous); phenol-β-D-glucosyltransferase; UDP glucosyltransferase (ambiguous); UDP-glucose glucosyltransferase (ambiguous); uridine diphosphoglucosyltransferase

Systematic name:

UDP-glucose:phenol β-D-glucosyltransferase

Comments:

Acts on a wide range of phenols.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9046-69-9

References:

1.	Dutton, G.J. Uridine diphosphate glucose and the synthesis of phenolic glucosides by mollusks. Arch. Biochem. Biophys. 116 (1966) 399–405. [DOI] [PMID: 5961845]

[EC 2.4.1.35 created 1972]

2.4.1.36

Accepted name:

α,α-trehalose-phosphate synthase (GDP-forming)

Reaction:

GDP-glucose + glucose 6-phosphate = GDP + α,α-trehalose 6-phosphate

Other name(s):

GDP-glucose—glucose-phosphate glucosyltransferase; guanosine diphosphoglucose-glucose phosphate glucosyltransferase; trehalose phosphate synthase (GDP-forming)

Systematic name:

GDP-glucose:D-glucose-6-phosphate 1-α-D-glucosyltransferase

Comments:

See also EC 2.4.1.15 [α,α-trehalose-phosphate synthase (UDP-forming)].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37257-32-2

References:

1.	Elbein, A.D. Carbohydrate metabolism in Streptomyces hygroscopicus. I. Enzymatic synthesis of trehalose phosphate from guanosine diphosphate D-glucose-14C. J. Biol. Chem. 242 (1967) 403–406. [PMID: 6022837]

[EC 2.4.1.36 created 1972]

2.4.1.37

Accepted name:

fucosylgalactoside 3-α-galactosyltransferase

Reaction:

UDP-α-D-galactose + α-L-fucosyl-(1→2)-D-galactosyl-R = UDP + α-D-galactosyl-(1→3)-[α-L-fucosyl(1→2)]-D-galactosyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)

Other name(s):

UDP-galactose:O-α-L-fucosyl(1→2)D-galactose α-D-galactosyltransferase; UDPgalactose:glycoprotein-α-L-fucosyl-(1,2)-D-galactose 3-α-D-galactosyltransferase; [blood group substance] α-galactosyltransferase; blood-group substance B-dependent galactosyltransferase; glycoprotein-fucosylgalactoside α-galactosyltransferase; histo-blood group B transferase; histo-blood substance B-dependent galactosyltransferase; UDP-galactose:α-L-fucosyl-1,2-D-galactoside 3-α-D-galactosyltransferase; UDP-galactose:α-L-fucosyl-(1→2)-D-galactoside 3-α-D-galactosyltransferase

Systematic name:

UDP-α-D-galactose:α-L-fucosyl-(1→2)-D-galactoside 3-α-D-galactosyltransferase

Comments:

Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37257-33-3

References:

1.	Race, C., Ziderman, D. and Watkins, W.M. An α-D-galactosyltransferase associated with the blood-group B character. Biochem. J. 107 (1968) 733–735. [PMID: 16742598]

[EC 2.4.1.37 created 1972, modified 1999, modified 2002]

2.4.1.38

Accepted name:

β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase

Reaction:

UDP-α-D-galactose + N-acetyl-β-D-glucosaminylglycopeptide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminylglycopeptide

Other name(s):

UDP-galactose—glycoprotein galactosyltransferase; glycoprotein 4-β-galactosyl-transferase; β-N-acetyl-β1-4-galactosyltransferase; thyroid glycoprotein β-galactosyltransferase; glycoprotein β-galactosyltransferase; thyroid galactosyltransferase; uridine diphosphogalactose-glycoprotein galactosyltransferase; β-N-acetylglucosaminyl-glycopeptide β-1,4-galactosyltransferase; GalT; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide β-1,4-galactosyltransferase; UDP-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase

Systematic name:

UDP-α-D-galactose:N-acetyl-β-D-glucosaminylglycopeptide 4-β-galactosyltransferase

Comments:

Terminal N-acetyl-β-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by β-1,6-links to galactose residues; lower activity towards residues linked to galactose by β-1,3-links. A component of EC 2.4.1.22 (lactose synthase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37237-43-7

References:

1.	Beyer, T.A., Sadler, J.E., Rearick, J.I., Paulson, J.C. and Hill, R.L. Glucosyltransferases and their uses in assessing oligosaccharide structure and structure-function relationship. Adv. Enzymol. 52 (1981) 23–175. [PMID: 6784450]
2.	Blanken, W.M., Hooghwinkel, G.J.M. and van den Eijnden, D.H. Biosynthesis of blood-group I and i substances. Specificity of bovine colostrum β-N-acetyl-D-glucosaminide β1→4 galactosyltransferase. Eur. J. Biochem. 127 (1982) 547–552. [DOI] [PMID: 6816588]
3.	Blanken, W.M. and van den Eijnden, D.H. Biosynthesis of terminal Gal α 1→3Gal β 1→4GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide α 1→3-galactosyltransferase from calf thymus. J. Biol. Chem. 260 (1985) 12927–12934. [PMID: 3932335]
4.	Spiro, M.H. and Spiro, R.G. Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid galactosyltransferase. J. Biol. Chem. 243 (1968) 6529–6537. [PMID: 5726898]

[EC 2.4.1.38 created 1972, modified 1976, modified 1980, modified 1986]

2.4.1.39

Accepted name:

steroid N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + estradiol-17α 3-D-glucuronoside = UDP + 17α-(N-acetyl-D-glucosaminyl)-estradiol 3-D-glucuronoside

Other name(s):

hydroxy steroid acetylglucosaminyltransferase; steroid acetylglucosaminyltransferase; uridine diphosphoacetylglucosamine-steroid acetylglucosaminyltransferase

Systematic name:

UDP-N-acetyl-α-D-glucosamine:estradiol-17α-3-D-glucuronoside 17α-N-acetylglucosaminyltransferase

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-56-1

References:

1.	Collins, D.C., Jirku, H. and Layne, D.S. Steroid N-acetylglucosaminyl transferase. Localization and some properties of the enzyme in rabbit tissues. J. Biol. Chem. 243 (1968) 2928–2933. [PMID: 5660254]

[EC 2.4.1.39 created 1972]

2.4.1.300

Accepted name:

cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)

Reaction:

1-O-vanilloyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = vanillate + cyanidin 3,7-di-O-β-D-glucoside

For diagram of anthocyanidin glucoside biosynthesis, click here

Glossary:

vanillate = 4-hydroxy-3-methoxybenzoate
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium

Other name(s):

AA7GT

Systematic name:

1-O-vanilloyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 7-O-β-D-glucosyltransferase

Comments:

Isolated from the plant Delphinium grandiflorum (delphinium). Also acts on other anthocyanidins and with other acyl-glucose derivatives.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374–3389. [DOI] [PMID: 20971893]

[EC 2.4.1.300 created 2013]

2.4.1.301

Accepted name:

2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase

Reaction:

(1) UDP-α-D-kanosamine + 2′-deamino-2′-hydroxyneamine = UDP + kanamycin A
(2) UDP-α-D-kanosamine + neamine = UDP + kanamycin B
(3) UDP-α-D-kanosamine + paromamine = UDP + kanamycin C
(4) UDP-α-D-kanosamine + 2′-deamino-2′-hydroxyparomamine = UDP + kanamycin X

For diagram of kanamycin A biosynthesis, click here

Glossary:

neamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
paromamine = (1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
UDP-α-D-kanosamine = uridine 5′-[3-(3-amino-3-deoxy-α-D-glucopyranosyl) diphosphate]
kanamycin A = (1S,2R,3R,4S,6R)-4,6-diamino-3-(6-amino-6-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside
kanamycin B = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-α-D-glucopyranoside
kanamycin C = (1R,2S,3S,4R,6S)-4,6-diamino-3-(3-amino-3-deoxy-α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 2-amino-2-deoxy-α-D-glucopyranoside
kanamycin X = (1S,2R,3R,4S,6R)-4,6-diamino-3-(α-D-glucopyranosyloxy)-2-hydroxycyclohexyl 3-amino-3-deoxy-α-D-glucopyranoside

Other name(s):

kanE (gene name); kanM2 (gene name)

Systematic name:

UDP-α-D-kanosamine:2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase

Comments:

Involved in the biosynthetic pathway of kanamycins. The enzyme characterized from the bacterium Streptomyces kanamyceticus can also accept UDP-α-D-glucose with lower efficiency [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Kudo, F., Sucipto, H. and Eguchi, T. Enzymatic activity of a glycosyltransferase KanM2 encoded in the kanamycin biosynthetic gene cluster. J. Antibiot. (Tokyo) 62 (2009) 707–710. [DOI] [PMID: 19911031]
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 2.4.1.301 created 2013]

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]

2.4.1.303

Accepted name:

UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase

Reaction:

UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WbbD; WbbD β3Gal-transferase; UDP-Gal:GlcNAc-R β1,3-galactosyltransferase; UDP-Gal:GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase; UDP-Gal:GlcNAc-R galactosyltransferase

Systematic name:

UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-β-galactosyltransferase (configuration-inverting)

Comments:

The enzyme is involved in the the biosynthesis of the O-antigen repeating unit of Escherichia coli O7:K1 (VW187). Requires Mn²⁺. cf. EC 2.4.1.343, UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Riley, J.G., Menggad, M., Montoya-Peleaz, P.J., Szarek, W.A., Marolda, C.L., Valvano, M.A., Schutzbach, J.S. and Brockhausen, I. The wbbD gene of E. coli strain VW187 (O7:K1) encodes a UDP-Gal: GlcNAcα-pyrophosphate-R β1,3-galactosyltransferase involved in the biosynthesis of O7-specific lipopolysaccharide. Glycobiology 15 (2005) 605–613. [DOI] [PMID: 15625181]
2.	Brockhausen, I., Riley, J.G., Joynt, M., Yang, X. and Szarek, W.A. Acceptor substrate specificity of UDP-Gal: GlcNAc-R β1,3-galactosyltransferase (WbbD) from Escherichia coli O7:K1. Glycoconj. J. 25 (2008) 663–673. [DOI] [PMID: 18536883]

[EC 2.4.1.303 created 2013, modified 2017]

2.4.1.304

Accepted name:

UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase

Reaction:

UDP-α-D-galactose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Gal-(1→4)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WfeD; UDP-Gal:GlcNAc-R 1,4-Gal-transferase; UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-galactosyltransferase

Systematic name:

UDP-α-D-galactose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,4-galactosyltransferase

Comments:

The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Shigella boydii B14. The activity is stimulated by Mn²⁺ or to a lesser extent by Mg²⁺, Ca²⁺, Ni²⁺ or Pb²⁺.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

Xu, C., Liu, B., Hu, B., Han, Y., Feng, L., Allingham, J.S., Szarek, W.A., Wang, L. and Brockhausen, I. Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid β-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14 that catalyzes the second step in O-antigen repeating-unit synthesis. J. Bacteriol. 193 (2011) 449–459. [DOI] [PMID: 21057010]

[EC 2.4.1.304 created 2013]

2.4.1.305

Accepted name:

UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase

Reaction:

UDP-α-D-glucose + N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + β-D-Glc-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WfaP; WfgD; UDP-Glc:GlcNAc-pyrophosphate-lipid β-1,3-glucosyltransferase; UDP-Glc:GlcNAc-diphosphate-lipid β-1,3-glucosyltransferase

Systematic name:

UDP-α-D-glucose:N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol β-1,3-glucosyltransferase

Comments:

The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O56 and serotype O152.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Brockhausen, I., Hu, B., Liu, B., Lau, K., Szarek, W.A., Wang, L. and Feng, L. Characterization of two β-1,3-glucosyltransferases from Escherichia coli serotypes O56 and O152. J. Bacteriol. 190 (2008) 4922–4932. [DOI] [PMID: 18487334]

[EC 2.4.1.305 created 2013]

2.4.1.306

Accepted name:

UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-galactosamine + N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WbnH

Systematic name:

UDP-N-acetyl-α-D-galactosamine:N-acetyl-α-D-galactosaminyl-diphospho-ditrans,octacis-undecaprenol α-1,3-N-acetyl-D-galactosyltransferase

Comments:

The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of Escherichia coli serotype O86.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Yi, W., Yao, Q., Zhang, Y., Motari, E., Lin, S. and Wang, P.G. The wbnH gene of Escherichia coli O86:H₂ encodes an α-1,3-N-acetylgalactosaminyl transferase involved in the O-repeating unit biosynthesis. Biochem. Biophys. Res. Commun. 344 (2006) 631–639. [DOI] [PMID: 16630548]

[EC 2.4.1.306 created 2013]

2.4.1.307

Deleted entry:

UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. Now included in EC 2.4.1.122, glycoprotein-N-acetylgalactosamine β-1,3-galactosyltransferase

[EC 2.4.1.307 created 2013, deleted 2016]

2.4.1.308

Accepted name:

GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase

Reaction:

GDP-β-L-fucose + β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = GDP + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WbnK

Systematic name:

GDP-β-L-fucose:β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,2-fucosyltransferase

Comments:

The enzyme is involved in the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040–2041. [DOI] [PMID: 15713070]
2.	Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]

[EC 2.4.1.308 created 2013]

2.4.1.309

Accepted name:

UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase

Reaction:

UDP-α-D-galactose + α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol = UDP + α-D-Gal-(1→3)-(α-L-Fuc-(1→2))-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol

Other name(s):

WbnI

Systematic name:

UDP-α-D-galactose:α-L-Fuc-(1→2)-β-D-Gal-(1→3)-α-D-GalNAc-(1→3)-α-D-GalNAc-diphospho-ditrans,octacis-undecaprenol α-1,3-galactosyltransferase

Comments:

The enzyme is involved in the the biosynthesis of the O-polysaccharide repeating unit of the bacterium Escherichia coli serotype O86.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yi, W., Shao, J., Zhu, L., Li, M., Singh, M., Lu, Y., Lin, S., Li, H., Ryu, K., Shen, J., Guo, H., Yao, Q., Bush, C.A. and Wang, P.G. Escherichia coli O86 O-antigen biosynthetic gene cluster and stepwise enzymatic synthesis of human blood group B antigen tetrasaccharide. J. Am. Chem. Soc. 127 (2005) 2040–2041. [DOI] [PMID: 15713070]
2.	Yi, W., Zhu, L., Guo, H., Li, M., Li, J. and Wang, P.G. Formation of a new O-polysaccharide in Escherichia coli O86 via disruption of a glycosyltransferase gene involved in O-unit assembly. Carbohydr. Res. 341 (2006) 2254–2260. [DOI] [PMID: 16839526]
3.	Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]

[EC 2.4.1.309 created 2013]

2.4.1.310

Accepted name:

vancomycin aglycone glucosyltransferase

Reaction:

UDP-α-D-glucose + vancomycin aglycone = UDP + devancosaminyl-vancomycin

For diagram of chloroorienticin biosynthesis, click here

Glossary:

devancosaminyl-vancomycin = vancomycin pseudoaglycone

Other name(s):

GtfB (ambiguous)

Systematic name:

UDP-α-D-glucose:vancomycin aglycone 48-O-β-glucosyltransferase

Comments:

The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745–4755. [DOI] [PMID: 11294642]
2.	Mulichak, A.M., Losey, H.C., Walsh, C.T. and Garavito, R.M. Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics. Structure 9 (2001) 547–557. [DOI] [PMID: 11470430]

[EC 2.4.1.310 created 2013]

2.4.1.311

Accepted name:

chloroorienticin B synthase

Reaction:

dTDP-β-L-4-epi-vancosamine + desvancosaminyl-vancomycin = dTDP + chloroorienticin B

For diagram of chloroorienticin biosynthesis, click here

Glossary:

dTDP-β-L-4-epi-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-methyl-β-L-arabino-hexopyranose
desvancosaminyl-vancomycin = vanomycin pseudoaglycone

Other name(s):

GtfA

Systematic name:

dTDP-L-4-epi-vancosamine:desvancosaminyl-vancomycin vancosaminyltransferase

Comments:

The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of the glycopeptide antibiotic chloroeremomycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Mulichak, A.M., Losey, H.C., Lu, W., Wawrzak, Z., Walsh, C.T. and Garavito, R.M. Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway. Proc. Natl. Acad. Sci. USA 100 (2003) 9238–9243. [DOI] [PMID: 12874381]
2.	Lu, W., Oberthur, M., Leimkuhler, C., Tao, J., Kahne, D. and Walsh, C.T. Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin. Proc. Natl. Acad. Sci. USA 101 (2004) 4390–4395. [DOI] [PMID: 15070728]

[EC 2.4.1.311 created 2013]

2.4.1.312

Accepted name:

protein O-mannose β-1,4-N-acetylglucosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-glucosamine + 3-O-(α-D-mannosyl)-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]

For diagram of glycoprotein biosynthesis, click here

Other name(s):

GTDC2 (gene name); POMGNT2

Systematic name:

UDP-N-acetyl-α-D-glucosamine:α-D-mannosyl-threonyl-[protein] 4-β-N-acetyl-D-glucosaminyltransferase

Comments:

The human protein is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]

[EC 2.4.1.312 created 2013]

2.4.1.313

Accepted name:

protein O-mannose β-1,3-N-acetylgalactosaminyltransferase

Reaction:

UDP-N-acetyl-α-D-galactosamine + 3-O-[N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein] = UDP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl-[protein]

For diagram of glycoprotein biosynthesis, click here

Other name(s):

B3GALNT2

Systematic name:

UDP-N-acetyl-α-D-galactosamine:N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl-threonyl-[protein] 3-β-N-acetyl-D-galactosaminyltransferase

Comments:

The human protein is specific for UDP-N-acetyl-α-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Hiruma, T., Togayachi, A., Okamura, K., Sato, T., Kikuchi, N., Kwon, Y.D., Nakamura, A., Fujimura, K., Gotoh, M., Tachibana, K., Ishizuka, Y., Noce, T., Nakanishi, H. and Narimatsu, H. A novel human β1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcβ1-3GlcNAc. J. Biol. Chem. 279 (2004) 14087–14095. [DOI] [PMID: 14724282]
2.	Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896–899. [DOI] [PMID: 23929950]

[EC 2.4.1.313 created 2013]

2.4.1.314

Accepted name:

ginsenoside Rd glucosyltransferase

Reaction:

UDP-α-D-glucose + ginsenoside Rd = UDP + ginsenoside Rb1

For diagram of protopanaxadiol ginsenosides ginsenosidases, click here

Glossary:

ginsenoside Rd = 20-(β-D-glucopyranosyl)oxy-3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol
ginsenoside Rb1 = 3β-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranosyloxy]-20-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyloxy]dammar-24-en-12β-ol

Other name(s):

UDPG:ginsenoside Rd glucosyltransferase; UDP-glucose:ginsenoside Rd glucosyltransferase; UGRdGT

Systematic name:

UDP-glucose:ginsenoside-Rd β-1,6-glucosyltransferase

Comments:

The glucosyl group forms a 1→6 bond to the glucosyloxy moiety at C-20 of ginsenoside Rd. Isolated from sanchi ginseng (Panax notoginseng).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Yue, C.-J. and Zhong J.-J. Purification and characterization of UDPG:ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng. Process Biochem. 40 (2005) 3742–3748.

[EC 2.4.1.314 created 2013]

2.4.1.315

Accepted name:

diglucosyl diacylglycerol synthase (1,6-linking)

Reaction:

(1) UDP-α-D-glucose + 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP
(2) UDP-α-D-glucose + 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol = 1,2-diacyl-3-O-[β-D-glucopyranosyl-(1→6)-β-D-glucopyranosyl-(1→6)-O-β-D-glucopyranosyl]-sn-glycerol + UDP

Other name(s):

monoglucosyl diacylglycerol (1→6) glucosyltransferase; MGlcDAG (1→6) glucosyltransferase; DGlcDAG synthase (ambiguous); UGT106B1; ypfP (gene name)

Systematic name:

UDP-α-D-glucose:1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol 6-glucosyltransferase

Comments:

The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose [1]. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo [3]. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1′-sn-glycerol) [2].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Jorasch, P., Wolter, F.P., Zahringer, U. and Heinz, E. A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29 (1998) 419–430. [DOI] [PMID: 9720862]
2.	Jorasch, P., Warnecke, D.C., Lindner, B., Zahringer, U. and Heinz, E. Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols. Eur. J. Biochem. 267 (2000) 3770–3783. [DOI] [PMID: 10848996]
3.	Andres, E., Martinez, N. and Planas, A. Expression and characterization of a Mycoplasma genitalium glycosyltransferase in membrane glycolipid biosynthesis: potential target against mycoplasma infections. J. Biol. Chem. 286 (2011) 35367–35379. [DOI] [PMID: 21835921]

[EC 2.4.1.315 created 2014]

2.4.1.316

Accepted name:

tylactone mycaminosyltransferase

Reaction:

tylactone + dTDP-α-D-mycaminose = dTDP + 5-O-β-D-mycaminosyltylactone

For diagram of tylactone biosynthesis, click here

Glossary:

tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyloxacyclohexadeca-11,13-diene-2,10-dione
dTDP-α-D-mycaminose = dTDP-3,6-dideoxy-3-dimethylamino-α-D-glucopyranose

Other name(s):

tylM2 (gene name)

Systematic name:

dTDP-α-D-mycaminose:tylactone 5-O-β-D-mycaminosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria. Activity is significantly enhanced by the presence of an accessory protein encoded by the tylM3 gene.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Gandecha, A.R., Large, S.L. and Cundliffe, E. Analysis of four tylosin biosynthetic genes from the tylLM region of the Streptomyces fradiae genome. Gene 184 (1997) 197–203. [DOI] [PMID: 9031628]
2.	Melancon, C.E., 3rd, Takahashi, H. and Liu, H.W. Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient glycosyltransfer in macrolide antibiotic biosynthesis. J. Am. Chem. Soc. 126 (2004) 16726–16727. [DOI] [PMID: 15612702]

[EC 2.4.1.316 created 2014]

2.4.1.317

Accepted name:

O-mycaminosyltylonolide 6-deoxyallosyltransferase

Reaction:

5-O-β-D-mycaminosyltylonolide + dTDP-6-deoxy-α-D-allose = dTDP + demethyllactenocin

For diagram of tylosin biosynthesis, click here

Glossary:

mycaminose = 3,6-dideoxy-3-dimethylamino-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxooxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-β-D-allopyranoside

Other name(s):

tylN (gene name)

Systematic name:

dTDP-6-deoxy-α-D-allose:5-O-β-D-mycaminosyltylonolide 23-O-6-deoxy-α-D-allosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Wilson, V.T. and Cundliffe, E. Characterization and targeted disruption of a glycosyltransferase gene in the tylosin producer, Streptomyces fradiae. Gene 214 (1998) 95–100. [DOI] [PMID: 9651492]

[EC 2.4.1.317 created 2014]

2.4.1.318

Accepted name:

demethyllactenocin mycarosyltransferase

Reaction:

dTDP-β-L-mycarose + demethyllactenocin = dTDP + demethylmacrocin

For diagram of tylosin biosynthesis, click here

Glossary:

dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
demethyllactenocin = [(2R,3R,4E,6E,9R,11R,12S,13S,14R)-12-{[3,6-dideoxy-3-(dimethylamino)-D-glucopyranosyl]oxy}-2-ethyl-14-hydroxy-5,9,13-trimethyl-8,16-dioxo-11-(2-oxoethyl)oxacyclohexadeca-4,6-dien-3-yl]methyl 6-deoxy-D-allopyranoside

Other name(s):

tylCV (gene name); tylC5 (gene name)

Systematic name:

dTDP-β-L-mycarose:demethyllactenocin 4′-O-α-L-mycarosyltransferase

Comments:

The enzyme participates in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Bate, N., Butler, A.R., Smith, I.P. and Cundliffe, E. The mycarose-biosynthetic genes of Streptomyces fradiae, producer of tylosin. Microbiology 146 (2000) 139–146. [DOI] [PMID: 10658660]

[EC 2.4.1.318 created 2014]

2.4.1.319

Accepted name:

β-1,4-mannooligosaccharide phosphorylase

Reaction:

[(1→4)-β-D-mannosyl]_n + phosphate = [(1→4)-β-D-mannosyl]_n-1 + α-D-mannose 1-phosphate

Other name(s):

RaMP2

Systematic name:

1,4-β-D-mannooligosaccharide:phosphate α-D-mannosyltransferase

Comments:

The enzyme, isolated from the ruminal bacterium Ruminococcus albus, catalyses the reversible phosphorolysis of β-1,4-mannooligosaccharide with a minimum size of three monomers.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Kawahara, R., Saburi, W., Odaka, R., Taguchi, H., Ito, S., Mori, H. and Matsui, H. Metabolic mechanism of mannan in a ruminal bacterium, Ruminococcus albus, involving two mannoside phosphorylases and cellobiose 2-epimerase: discovery of a new carbohydrate phosphorylase, β-1,4-mannooligosaccharide phosphorylase. J. Biol. Chem. 287 (2012) 42389–42399. [DOI] [PMID: 23093406]

[EC 2.4.1.319 created 2014]

2.4.1.320

Accepted name:

1,4-β-mannosyl-N-acetylglucosamine phosphorylase

Reaction:

4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + α-D-mannose 1-phosphate

Other name(s):

BT1033

Systematic name:

4-O-β-D-mannopyranosyl-N-acetyl-D-glucosamine:phosphate α-D-mannosyltransferase

Comments:

The enzyme isolated from the anaerobic bacterium Bacteroides thetaiotaomicron is involved in the degradation of host-derived N-glycans.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Nihira, T., Suzuki, E., Kitaoka, M., Nishimoto, M., Ohtsubo, K. and Nakai, H. Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans. J. Biol. Chem. 288 (2013) 27366–27374. [DOI] [PMID: 23943617]

[EC 2.4.1.320 created 2014]

2.4.1.321

Accepted name:

cellobionic acid phosphorylase

Reaction:

4-O-β-D-glucopyranosyl-D-gluconate + phosphate = α-D-glucose 1-phosphate + D-gluconate

Glossary:

4-O-β-D-glucopyranosyl-D-gluconate = cellobionate

Systematic name:

4-O-β-D-glucopyranosyl-D-gluconate:phosphate α-D-glucosyltransferase

Comments:

The enzyme occurs in cellulolytic bacteria and fungi. It catalyses the reversible phosphorolysis of cellobionic acid. In the synthetic direction it produces 4-O-β-D-glucopyranosyl-D-glucuronate from α-D-glucose 1-phosphate and D-glucuronate with low activity

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Nihira, T., Saito, Y., Nishimoto, M., Kitaoka, M., Igarashi, K., Ohtsubo, K. and Nakai, H. Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi. FEBS Lett. 587 (2013) 3556–3561. [DOI] [PMID: 24055472]

[EC 2.4.1.321 created 2014]

2.4.1.322

Accepted name:

devancosaminyl-vancomycin vancosaminetransferase

Reaction:

dTDP-β-L-vancosamine + devancosaminyl-vancomycin = dTDP + vancomycin

For diagram of chloroorienticin biosynthesis, click here

Glossary:

dTDP-β-L-vancosamine = dTDP-3-amino-2,3,6-trideoxy-3-C-methyl-β-L-lyxo-hexopyranose

Other name(s):

devancosaminyl-vancomycin TDP-vancosaminyltransferase; GtfD; dTDP-β-L-vancomycin:desvancosaminyl-vancomycin β-L-vancosaminetransferase; desvancosaminyl-vancomycin vancosaminetransferase

Systematic name:

dTDP-β-L-vancomycin:devancosaminyl-vancomycin β-L-vancosaminetransferase

Comments:

The enzyme, isolated from the bacterium Amycolatopsis orientalis, catalyses the ultimate step in the biosynthesis of the antibiotic vancomycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Losey, H.C., Peczuh, M.W., Chen, Z., Eggert, U.S., Dong, S.D., Pelczer, I., Kahne, D. and Walsh, C.T. Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides. Biochemistry 40 (2001) 4745–4755. [DOI] [PMID: 11294642]
2.	Mulichak, A.M., Lu, W., Losey, H.C., Walsh, C.T. and Garavito, R.M. Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43 (2004) 5170–5180. [DOI] [PMID: 15122882]

[EC 2.4.1.322 created 2014]

2.4.1.323

Accepted name:

7-deoxyloganetic acid glucosyltransferase

Reaction:

UDP-α-D-glucose + 7-deoxyloganetate = UDP + 7-deoxyloganate

For diagram of secologanin biosynthesis, click here

Other name(s):

UGT8

Systematic name:

UDP-α-D-glucose:7-deoxyloganetate O-D-glucosyltransferase

Comments:

Isolated from the plant Catharanthus roseus (Madagascar periwinkle). Involved in loganin and secologanin biosynthesis. Does not react with 7-deoxyloganetin. cf. EC 2.4.1.324 7-deoxyloganetin glucosyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Asada, K., Salim, V., Masada-Atsumi, S., Edmunds, E., Nagatoshi, M., Terasaka, K., Mizukami, H. and De Luca, V. A 7-deoxyloganetic acid glucosyltransferase contributes a key step in secologanin biosynthesis in madagascar periwinkle. Plant Cell 25 (2013) 4123–4134. [DOI] [PMID: 24104568]

[EC 2.4.1.323 created 2014]

2.4.1.324

Accepted name:

7-deoxyloganetin glucosyltransferase

Reaction:

UDP-α-D-glucose + 7-deoxyloganetin = UDP + 7-deoxyloganin

For diagram of secologanin biosynthesis, click here

Other name(s):

UDPglucose:iridoid glucosyltransferase; UGT6; UGT85A24

Systematic name:

UDP-α-D-glucose:7-deoxyloganetin O-D-glucosyltransferase

Comments:

Isolated from the plants Catharanthus roseus (Madagascar periwinkle) and Gardenia jasminoides (cape jasmine). With Gardenia it also acts on genipin. Involved in loganin and secologanin biosynthesis. Does not react with 7-deoxyloganetate. cf. EC 2.4.1.323 7-deoxyloganetic acid glucosyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Nagatoshi, M., Terasaka, K., Nagatsu, A. and Mizukami, H. Iridoid-specific glucosyltransferase from Gardenia jasminoides. J. Biol. Chem. 286 (2011) 32866–32874. [DOI] [PMID: 21799001]
2.	Asada, K., Salim, V., Masada-Atsumi, S., Edmunds, E., Nagatoshi, M., Terasaka, K., Mizukami, H. and De Luca, V. A 7-deoxyloganetic acid glucosyltransferase contributes a key step in secologanin biosynthesis in madagascar periwinkle. Plant Cell 25 (2013) 4123–4134. [DOI] [PMID: 24104568]

[EC 2.4.1.324 created 2014]

2.4.1.325

Accepted name:

TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase

Reaction:

dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Glossary:

dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol

Other name(s):

TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)

Systematic name:

dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase

Comments:

Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509–6516. [DOI] [PMID: 11673418]

[EC 2.4.1.325 created 2014]

2.4.1.326

Accepted name:

aklavinone 7-L-rhodosaminyltransferase

Reaction:

dTDP-β-L-rhodosamine + aklavinone = dTDP + aclacinomycin T

For diagram of aklavinone biosynthesis, click here

Glossary:

dTDP-β-L-rhodosamine = dTDP-2,3,6-trideoxy-3-dimethylamino-β-L-lyxo-hexose
aklavinone = methyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate
aclacinomycin T = 7-O-(α-L-rhodosaminyl)aklavinone

Other name(s):

AknS/AknT; aklavinone 7-β-L-rhodosaminyltransferase; dTDP-β-L-rhodosamine:aklavinone 7-α-L-rhodosaminyltransferase

Systematic name:

dTDP-β-L-rhodosamine:aklavinone 7-α-L-rhodosaminyltransferase (configuration-inverting)

Comments:

Isolated from the bacterium Streptomyces galilaeus. Forms a complex with its accessory protein AknT, and has very low activity in its absence. The enzyme can also use dTDP-2-deoxy-β-L-fucose. Involved in the biosynthesis of other aclacinomycins.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Lu, W., Leimkuhler, C., Gatto, G.J., Jr., Kruger, R.G., Oberthur, M., Kahne, D. and Walsh, C.T. AknT is an activating protein for the glycosyltransferase AknS in L-aminodeoxysugar transfer to the aglycone of aclacinomycin A. Chem. Biol. 12 (2005) 527–534. [DOI] [PMID: 15911373]
2.	Leimkuhler, C., Fridman, M., Lupoli, T., Walker, S., Walsh, C.T. and Kahne, D. Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A. J. Am. Chem. Soc. 129 (2007) 10546–10550. [DOI] [PMID: 17685523]

[EC 2.4.1.326 created 2014, modified 2015]

2.4.1.327

Accepted name:

aclacinomycin-T 2-deoxy-L-fucose transferase

Reaction:

dTDP-2-deoxy-β-L-fucose + aclacinomycin T = dTDP + aclacinomycin S

For diagram of aclacinomycin A and Y biosynthesis, click here

Glossary:

idarubicin = (7S,9S)-9-acetyl-7-(3-amino-2,3,6-trideoxy-β-L-lyxo-hexosyloxy)-6,9,11-trihydroxy-7,8,9,10-tetrahydrotetracene-5,12-dione
aclacinomycin S = 7-O-(2-deoxy-α-L-fucosyl-(1→4)-rhodosaminyl)aklavinone
aclacinomycin T = 7-O-(α-L-rhodosaminyl)aklavinone

Other name(s):

AknK

Systematic name:

dTDP-2-deoxy-β-L-fucose:7-(α-L-rhodosaminyl)aklavinone 2-deoxy-α-L-fucosyltransferase

Comments:

The enzyme, isolated from the bacterium Streptomyces galilaeus, is involved in the biosynthesis of other aclacinomycins. Also acts on idarubicin. It will slowly add a second 2-deoxy-L-fucose unit to aclacinomycin S in vitro.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Lu, W., Leimkuhler, C., Oberthur, M., Kahne, D. and Walsh, C.T. AknK is an L-2-deoxyfucosyltransferase in the biosynthesis of the anthracycline aclacinomycin A. Biochemistry 43 (2004) 4548–4558. [DOI] [PMID: 15078101]

[EC 2.4.1.327 created 2014]

2.4.1.328

Accepted name:

erythronolide mycarosyltransferase

Reaction:

dTDP-β-L-mycarose + erythronolide B = dTDP + 3-α-L-mycarosylerythronolide B

For diagram of erythromycin biosynthesis, click here

Glossary:

dTDP-β-L-mycarose = dTDP-2,6-dideoxy-3-C-methyl-β-L-ribo-hexose
L-mycarose = 2,6-dideoxy-3-C-methyl-L-ribo-hexose

Other name(s):

EryBV

Systematic name:

dTDP-β-L-mycarose:erythronolide B L-mycarosyltransferase

Comments:

Isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Zhang, C., Fu, Q., Albermann, C., Li, L. and Thorson, J.S. The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification. ChemBioChem 8 (2007) 385–390. [DOI] [PMID: 17262863]

[EC 2.4.1.328 created 2014]

2.4.1.329

Accepted name:

sucrose 6^F-phosphate phosphorylase

Reaction:

sucrose 6^F-phosphate + phosphate = α-D-glucopyranose 1-phosphate + β-D-fructofuranose 6-phosphate

Other name(s):

sucrose 6′-phosphate phosphorylase

Systematic name:

sucrose 6^F-phosphate:phosphate 1-α-D-glucosyltransferase

Comments:

The enzyme, isolated from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum, catalyses the reversible phosphorolysis of sucrose 6^F-phosphate. It also acts on sucrose with lower activity.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Verhaeghe, T., Aerts, D., Diricks, M., Soetaert, W. and Desmet, T. The quest for a thermostable sucrose phosphorylase reveals sucrose 6′-phosphate phosphorylase as a novel specificity. Appl. Microbiol. Biotechnol. 98 (2014) 7027–7037. [DOI] [PMID: 24599311]

[EC 2.4.1.329 created 2014]

2.4.1.330

Accepted name:

β-D-glucosyl crocetin β-1,6-glucosyltransferase

Reaction:

(1) UDP-α-D-glucose + β-D-glucosyl crocetin = UDP + β-D-gentiobiosyl crocetin
(2) UDP-α-D-glucose + bis(β-D-glucosyl) crocetin = UDP + β-D-gentiobiosyl β-D-glucosyl crocetin
(3) UDP-α-D-glucose + β-D-gentiobiosyl β-D-glucosyl crocetin = UDP + crocin

For diagram of crocin biosynthesis, click here

Glossary:

crocin = bis(β-D-gentiobiosyl) crocetin
crocetin = (2E,4E,6E,8E,10E,12E,14E)-2,6,11,15-tetramethylhexadeca-2,4,6,8,10,12,14-heptaenedioate

Other name(s):

UGT94E5; UDP-glucose:crocetin glucosyl ester glucosyltransferasee

Systematic name:

UDP-α-D-glucose:β-D-glucosyl crocetin β-1,6-glucosyltransferase

Comments:

The enzyme, characterized from the plant Gardenia jasminoides, adds a glucose to several crocetin glycosyl esters, but not to crocetin (cf. EC 2.4.1.271, crocetin glucosyltransferase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Nagatoshi, M., Terasaka, K., Owaki, M., Sota, M., Inukai, T., Nagatsu, A. and Mizukami, H. UGT75L6 and UGT94E5 mediate sequential glucosylation of crocetin to crocin in Gardenia jasminoides. FEBS Lett. 586 (2012) 1055–1061. [DOI] [PMID: 22569263]

[EC 2.4.1.330 created 2014]

2.4.1.331

Accepted name:

8-demethyltetracenomycin C L-rhamnosyltransferase

Reaction:

dTDP-β-L-rhamnose + 8-demethyltetracenomycin C = dTDP + 8-demethyl-8-α-L-rhamnosyltetracenomycin C

For diagram of elloramycin biosynthesis, click here

Glossary:

dTDP-β-L-rhamnose = dTDP-6-deoxy-β-L-mannose

Other name(s):

elmGT

Systematic name:

dTDP-β-L-rhamnose:8-demethyltetracenomycin C 3-α-L-rhamnosyltransferase

Comments:

Isolated from Streptomyces olivaceus Tü2353. Involved in elloramycin biosynthesis. In vitro it can also utilize other 6-deoxy D- or L-hexoses.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Blanco, G., Patallo, E.P., Brana, A.F., Trefzer, A., Bechthold, A., Rohr, J., Mendez, C. and Salas, J.A. Identification of a sugar flexible glycosyltransferase from Streptomyces olivaceus, the producer of the antitumor polyketide elloramycin. Chem. Biol. 8 (2001) 253–263. [DOI] [PMID: 11306350]

[EC 2.4.1.331 created 2014]

2.4.1.332

Accepted name:

1,2-α-glucosylglycerol phosphorylase

Reaction:

2-O-α-D-glucopyranosyl-glycerol + phosphate = β-D-glucose 1-phosphate + glycerol

Other name(s):

2-O-α-D-glucopyranosylglycerol phosphorylase

Systematic name:

2-O-α-D-glucopyranosyl-glycerol:phosphate β-D-glucosyltransferase

Comments:

The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Nihira, T., Saito, Y., Ohtsubo, K., Nakai, H. and Kitaoka, M. 2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate. PLoS One 9:e86548 (2014). [DOI] [PMID: 24466148]
2.	Touhara, K.K., Nihira, T., Kitaoka, M., Nakai, H. and Fushinobu, S. Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase. J. Biol. Chem. 289 (2014) 18067–18075. [DOI] [PMID: 24828502]

[EC 2.4.1.332 created 2014]

2.4.1.333

Accepted name:

1,2-β-oligoglucan phosphorylase

Reaction:

[(1→2)-β-D-glucosyl]_n + phosphate = [(1→2)-β-D-glucosyl]_n-1 + α-D-glucose 1-phosphate

Systematic name:

1,2-β-D-glucan:phosphate α-D-glucosyltransferase

Comments:

The enzyme has been isolated from the bacterium Listeria innocua. It catalyses the reversible phosphorolysis of β-(1→2)-D-glucans. The minimum length of the substrate for the phosphorolytic reaction is 3 D-glucose units. In the synthetic reaction starting from sophorose and α-D-glucose 1-phosphate the average polymerisation degree is 39.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Nakajima, M., Toyoizumi, H., Abe, K., Nakai, H., Taguchi, H. and Kitaoka, M. 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One 9:e92353 (2014). [DOI] [PMID: 24647662]

[EC 2.4.1.333 created 2014]

2.4.1.334

Accepted name:

1,3-α-oligoglucan phosphorylase

Reaction:

[(1→3)-α-D-glucosyl]_n + phosphate = [(1→3)-α-D-glucosyl]_n-1 + β-D-glucose 1-phosphate

Systematic name:

1,3-α-D-glucan:phosphate β-D-glucosyltransferase

Comments:

The enzyme, isolated from the bacterium Clostridium phytofermentans, catalyses a reversible reaction. Substrates for the phosphorolytic reaction are α-1,3-linked oligoglucans with a polymerisation degree of 3 or more. Nigerose (i.e. 3-O-α-D-glucopyranosyl-D-glucopyranose) is not phosphorylyzed but can serve as substrate in the reverse direction (cf. EC 2.4.1.279, nigerose phosphorylase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Nihira, T., Nishimoto, M., Nakai, H., Ohtsubo, K., and Kitaoka, M. Characterization of two phosphorylases for α-1,3-oligoglucans from Clostridium phytofermentans. J. Appl. Glycosci. 61 (2014) 59–66.

[EC 2.4.1.334 created 2014]

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]

2.4.1.336

Accepted name:

monoglucosyldiacylglycerol synthase

Reaction:

UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol

Glossary:

a 1,2-diacyl-3-O-(β-D-glucopyranosyl)-sn-glycerol = a β-monoglucosyldiacylglycerol = a GlcDG

Other name(s):

mgdA (gene name)

Systematic name:

UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-β-D-glucosyltransferase

Comments:

The enzymes from cyanobacteria are involved in the biosynthesis of galactolipids found in their photosynthetic membranes. The enzyme belongs to the GT2 family of configuration-inverting glycosyltranferases [2]. cf. EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Sato, N. and Murata, N. Lipid biosynthesis in the blue-green-alga (cyanobacterium), Anabaena variabilis. 3. UDP-glucose-diacylglycerol glucosyltransferase activity in vitro. Plant Cell Physiol. 23 (1982) 1115–1120.
2.	Awai, K., Kakimoto, T., Awai, C., Kaneko, T., Nakamura, Y., Takamiya, K., Wada, H. and Ohta, H. Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria. Plant Physiol. 141 (2006) 1120–1127. [DOI] [PMID: 16714404]
3.	Yuzawa, Y., Shimojima, M., Sato, R., Mizusawa, N., Ikeda, K., Suzuki, M., Iwai, M., Hori, K., Wada, H., Masuda, S. and Ohta, H. Cyanobacterial monogalactosyldiacylglycerol-synthesis pathway is involved in normal unsaturation of galactolipids and low-temperature adaptation of Synechocystis sp. PCC 6803. Biochim. Biophys. Acta 1841 (2014) 475–483. [DOI] [PMID: 24370445]

[EC 2.4.1.336 created 2015]

2.4.1.337

Accepted name:

1,2-diacylglycerol 3-α-glucosyltransferase

Reaction:

UDP-α-D-glucose + a 1,2-diacyl-sn-glycerol = UDP + a 1,2-diacyl-3-O-(α-D-glucopyranosyl)-sn-glycerol

Other name(s):

mgs (gene name); UDP-glucose:diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol glucosyltransferase; uridine diphosphoglucose-diacylglycerol glucosyltransferase; UDP-glucose-diacylglycerol glucosyltransferase; UDP-glucose:1,2-diacylglycerol 3-D-glucosyltransferase; UDP-glucose:1,2-diacyl-sn-glycerol 3-D-glucosyltransferase; 1,2-diacylglycerol 3-glucosyltransferase (ambiguous)

Systematic name:

UDP-α-D-glucose:1,2-diacyl-sn-glycerol 3-α-D-glucosyltransferase

Comments:

The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC 2.4.1.336, monoglucosyldiacylglycerol synthase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Karlsson, O.P., Dahlqvist, A., Vikstrom, S. and Wieslander, A. Lipid dependence and basic kinetics of the purified 1,2-diacylglycerol 3-glucosyltransferase from membranes of Acholeplasma laidlawii. J. Biol. Chem. 272 (1997) 929–936. [DOI] [PMID: 8995384]
2.	Li, L., Storm, P., Karlsson, O.P., Berg, S. and Wieslander, A. Irreversible binding and activity control of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer surface. Biochemistry 42 (2003) 9677–9686. [DOI] [PMID: 12911309]
3.	Berg, S., Edman, M., Li, L., Wikstrom, M. and Wieslander, A. Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes. Recognition of a large group of lipid glycosyltransferases in eubacteria and archaea. J. Biol. Chem. 276 (2001) 22056–22063. [DOI] [PMID: 11294844]
4.	Semeniuk, A., Sohlenkamp, C., Duda, K. and Holzl, G. A bifunctional glycosyltransferase from Agrobacterium tumefaciens synthesizes monoglucosyl and glucuronosyl diacylglycerol under phosphate deprivation. J. Biol. Chem. 289 (2014) 10104–10114. [DOI] [PMID: 24558041]

[EC 2.4.1.337 created 2015]

2.4.1.338

Accepted name:

validoxylamine A glucosyltransferase

Reaction:

UDP-α-D-glucose + validoxylamine A = UDP + validamycin A

For diagram of validamycin biosynthesis, click here

Glossary:

validoxylamine A = (1S,2S,3R,6S)-4-(hydroxymethyl)-6-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol

Other name(s):

vldK (gene name); valG (gene name)

Systematic name:

UDP-α-D-glucose:validoxylamine-A 4′-O-glucosyltransferase

Comments:

The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Bai, L., Li, L., Xu, H., Minagawa, K., Yu, Y., Zhang, Y., Zhou, X., Floss, H.G., Mahmud, T. and Deng, Z. Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A. Chem. Biol. 13 (2006) 387–397. [DOI] [PMID: 16632251]
2.	Xu, H., Minagawa, K., Bai, L., Deng, Z. and Mahmud, T. Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4′′-epi-validamycin A. J Nat Prod 71 (2008) 1233–1236. [DOI] [PMID: 18563934]

[EC 2.4.1.338 created 2016]