ExplorEnz: EC 2.3.1.20*

Your query returned 11 entries. Printable version

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, PDB, 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]

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]

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]

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, PDB

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]

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]

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, PDB

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]

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]

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, PDB

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]

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]

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]

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]