The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 2.3.1.20     
Accepted name: diacylglycerol O-acyltransferase
Reaction: acyl-CoA + 1,2-diacyl-sn-glycerol = CoA + triacylglycerol
Other name(s): diglyceride acyltransferase; 1,2-diacylglycerol acyltransferase; diacylglycerol acyltransferase; diglyceride O-acyltransferase; palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase; acyl-CoA:1,2-diacylglycerol O-acyltransferase
Systematic name: acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Comments: Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-98-5
References:
1.  Coleman, R. and Bell, R.M. Triacylglycerol synthesis in isolated fat cells. Studies on the microsomal diacylglycerol acyltransferase activity using ethanol-dispersed diacylglycerols. J. Biol. Chem. 251 (1976) 4537–4543. [PMID: 947894]
2.  Grigor, M.R. and Bell, R.M. Separate monoacylglycerol and diacylglycerol acyltransferases function in intestinal triacylglycerol synthesis. Biochim. Biophys. Acta 712 (1982) 464–472. [DOI] [PMID: 6289909]
3.  Kawasaki, T. and Snyder, F. Synthesis of a novel acetylated neutral lipid related to platelet-activating factor by acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol acyltransferase in HL-60 cells. J. Biol. Chem. 263 (1988) 2593–2596. [PMID: 3422635]
4.  Weiss, S.B., Kennedy, E.P. and Kiyasu, J.Y. The enzymatic synthesis of triglycerides. J. Biol. Chem. 235 (1960) 40–44. [PMID: 13843753]
[EC 2.3.1.20 created 1965]
 
 
EC 2.3.1.200     
Accepted name: lipoyl amidotransferase
Reaction: [glycine cleavage system H]-N6-lipoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N6-lipoyl-L-lysine
Glossary: lipoic acid = 5-[(3R)-1,2-dithiolan-3-yl]pentanoic acid
Other name(s): LipL (gene name, ambiguous)
Systematic name: [glycine cleavage system H]-N6-lipoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine lipoyltransferase
Comments: In the bacterium Listeria monocytogenes the enzyme takes part in a pathway for scavenging of lipoic acid. The enzyme is bound to 2-oxo-acid dehydrogenases such as the pyruvate dehydrogenase complex, where it transfers the lipoyl moiety from lipoyl-[glycine cleavage system H] to the E2 subunits of the complexes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Christensen, Q.H., Hagar, J.A., O'Riordan, M.X. and Cronan, J.E. A complex lipoate utilization pathway in Listeria monocytogenes. J. Biol. Chem. 286 (2011) 31447–31456. [DOI] [PMID: 21768091]
[EC 2.3.1.200 created 2012]
 
 
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 2.3.1.202     
Accepted name: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
Reaction: acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine = CoA + UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose
Other name(s): PseH
Systematic name: acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase
Comments: Isolated from Helicobacter pylori. The enzyme is involved in the biosynthesis of pseudaminic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C–14C. [DOI] [PMID: 16751642]
[EC 2.3.1.202 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
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 2.3.1.204     
Accepted name: octanoyl-[GcvH]:protein N-octanoyltransferase
Reaction: [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
Glossary: GcvH = glycine cleavage system H]
Other name(s): LipL; octanoyl-[GcvH]:E2 amidotransferase; ywfL (gene name)
Systematic name: [glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase
Comments: In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Christensen, Q.H., Martin, N., Mansilla, M.C., de Mendoza, D. and Cronan, J.E. A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol. Microbiol. 80 (2011) 350–363. [DOI] [PMID: 21338421]
2.  Martin, N., Christensen, Q.H., Mansilla, M.C., Cronan, J.E. and de Mendoza, D. A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis. Mol. Microbiol. 80 (2011) 335–349. [DOI] [PMID: 21338420]
[EC 2.3.1.204 created 2012]
 
 
EC 2.3.1.205     
Accepted name: fumigaclavine B O-acetyltransferase
Reaction: acetyl-CoA + fumigaclavine B = CoA + fumigaclavine A
For diagram of fumigaclavin alkaloid biosynthesis, click here
Glossary: fumigaclavine B = 6,8β-dimethylergolin-9-ol;
fumigaclavine A = 6,8β-dimethylergolin-9β-yl acetate
Other name(s): FgaAT
Systematic name: acetyl-CoA:fumigaclavine B O-acetyltransferase
Comments: The enzyme participates in the biosynthesis of fumigaclavine C, an ergot alkaloid produced by some fungi of the Trichocomaceae family.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, X., Wang, L., Steffan, N., Yin, W.B. and Li, S.M. Ergot alkaloid biosynthesis in Aspergillus fumigatus: FgaAT catalyses the acetylation of fumigaclavine B. ChemBioChem. 10 (2009) 2325–2328. [DOI] [PMID: 19672909]
[EC 2.3.1.205 created 2012]
 
 
EC 2.3.1.206     
Accepted name: 3,5,7-trioxododecanoyl-CoA synthase
Reaction: 3 malonyl-CoA + hexanoyl-CoA = 3 CoA + 3,5,7-trioxododecanoyl-CoA + 3 CO2
For diagram of cannabinoid biosynthesis, click here
Other name(s): TKS (ambiguous); olivetol synthase (incorrect)
Systematic name: malonyl-CoA:hexanoyl-CoA malonyltransferase (3,5,7-trioxododecanoyl-CoA-forming)
Comments: A polyketide synthase catalysing the first committed step in the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme was previously thought to also function as a cyclase, but the cyclization is now known to be catalysed by EC 4.4.1.26, olivetolic acid cyclase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Taura, F., Tanaka, S., Taguchi, C., Fukamizu, T., Tanaka, H., Shoyama, Y. and Morimoto, S. Characterization of olivetol synthase, a polyketide synthase putatively involved in cannabinoid biosynthetic pathway. FEBS Lett. 583 (2009) 2061–2066. [DOI] [PMID: 19454282]
2.  Gagne, S.J., Stout, J.M., Liu, E., Boubakir, Z., Clark, S.M. and Page, J.E. Identification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketides. Proc. Natl. Acad. Sci. USA 109 (2012) 12811–12816. [DOI] [PMID: 22802619]
[EC 2.3.1.206 created 2012]
 
 
EC 2.3.1.207     
Accepted name: β-ketodecanoyl-[acyl-carrier-protein] synthase
Reaction: octanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: [acyl-carrier protein] = [acp]
Systematic name: octanoyl-CoA:malonyl-[acyl-carrier protein] C-heptanoylltransferase (decarboxylating, CoA-forming)
Comments: This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via β-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for β-oxidation degradation intermediates into de novo fatty acid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yuan, Y., Leeds, J.A. and Meredith, T.C. Pseudomonas aeruginosa directly shunts β-oxidation degradation intermediates into de novo fatty acid biosynthesis. J. Bacteriol. 194 (2012) 5185–5196. [DOI] [PMID: 22753057]
[EC 2.3.1.207 created 2012]
 
 
EC 2.3.1.208     
Accepted name: 4-hydroxycoumarin synthase
Reaction: malonyl-CoA + 2-hydroxybenzoyl-CoA = 2 CoA + 4-hydroxycoumarin + CO2
For diagram of polyketides biosynthesis, click here
Glossary: 2-hydroxybenzoyl-CoA = salicyloyl-CoA
Other name(s): BIS2; BIS3
Systematic name: malonyl-CoA:2-hydroxybenzoyl-CoA malonyltransferase
Comments: The enzyme, a polyketide synthase, can also accept benzoyl-CoA as substrate, which it condenses with 3 malonyl-CoA molecules to form 3,5-dihydroxybiphenyl (cf. EC 2.3.1.177, biphenyl synthase) [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, B., Raeth, T., Beuerle, T. and Beerhues, L. A novel 4-hydroxycoumarin biosynthetic pathway. Plant Mol. Biol. 72 (2010) 17–25. [DOI] [PMID: 19757094]
[EC 2.3.1.208 created 2012]
 
 
EC 2.3.1.209     
Accepted name: dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
Reaction: acetyl-CoA + dTDP-4-amino-4,6-dideoxy-α-D-glucose = CoA + dTDP-4-acetamido-4,6-dideoxy-α-D-glucose
Other name(s): VioB
Systematic name: acetyl-CoA:dTDP-4-amino-4,6-dideoxy-α-D-glucose N-acetyltransferase
Comments: The non-activated product, 4-acetamido-4,6-dideoxy-α-D-glucose, is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, Y., Xu, Y., Perepelov, A.V., Qi, Y., Knirel, Y.A., Wang, L. and Feng, L. Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7. J. Bacteriol. 189 (2007) 8626–8635. [DOI] [PMID: 17905981]
[EC 2.3.1.209 created 2012]
 
 


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