The Enzyme Database

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EC 2.3.1.85     
Accepted name: fatty-acid synthase system
Reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+
Glossary: a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13–22 carbons.
Other name(s): FASN (gene name); fatty-acid synthase
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing and thioester-hydrolysing)
Comments: The animal enzyme is a multi-functional protein catalysing the reactions of EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41 β-ketoacyl-[acyl-carrier-protein] synthase I, EC 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase, EC 4.2.1.59 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 3.1.2.14 oleoyl-[acyl-carrier-protein] hydrolase. cf. EC 2.3.1.86, fatty-acyl-CoA synthase system.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-77-6
References:
1.  Stoops, J.K., Ross, P., Arslanian, M.J., Aune, K.C., Wakil, S.J. and Oliver, R.M. Physicochemical studies of the rat liver and adipose fatty acid synthetases. J. Biol. Chem. 254 (1979) 7418–7426. [PMID: 457689]
2.  Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537–579. [DOI] [PMID: 6137188]
[EC 2.3.1.85 created 1984, modified 2019]
 
 
EC 3.1.1.67     
Accepted name: fatty-acyl-ethyl-ester synthase
Reaction: a long-chain-fatty-acyl ethyl ester + H2O = a long-chain-fatty acid + ethanol
Glossary: a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13-22 carbons.
Other name(s): FAEES
Systematic name: long-chain-fatty-acyl-ethyl-ester acylhydrolase
Comments: The reaction, forms ethyl esters from fatty acids and ethanol in the absence of coenzyme A or ATP. Best substrates are unsaturated octadecanoic acids; palmitate, stearate and arachidonate also act, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 90119-16-7
References:
1.  Mogelson, S. and Lange, L.G. Nonoxidative ethanol metabolism in rabbit myocardium: purification to homogeneity of fatty acyl ethyl ester synthase. Biochemistry 23 (1984) 4075–4081. [PMID: 6487591]
[EC 3.1.1.67 created 1989]
 
 
EC 6.2.1.3     
Accepted name: long-chain-fatty-acid—CoA ligase
Reaction: ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA
Glossary: a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13-22 carbons.
Other name(s): acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1
Systematic name: long-chain fatty acid:CoA ligase (AMP-forming)
Comments: Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9013-18-7
References:
1.  Bakken, A.M. and Farstad, M. Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets. Biochem. J. 261 (1989) 71–76. [PMID: 2528345]
2.  Hosaka, K., Mishima, M., Tanaka, T., Kamiryo, T. and Numa, S. Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification, properties and immunochemical studies. Eur. J. Biochem. 93 (1979) 197–203. [DOI] [PMID: 108099]
3.  Nagamatsu, K., Soeda, S., Mori, M. and Kishimoto, Y. Lignoceroyl-coenzyme A synthetase from developing rat brain: partial purification, characterization and comparison with palmitoyl-coenzyme A synthetase activity and liver enzyme. Biochim. Biophys. Acta 836 (1985) 80–88. [DOI] [PMID: 3161545]
4.  Tanaka, T., Hosaka, K., Hoshimaru, M. and Numa, S. Purification and properties of long-chain acyl-coenzyme-A synthetase from rat liver. Eur. J. Biochem. 98 (1979) 165–172. [DOI] [PMID: 467438]
[EC 6.2.1.3 created 1961, modified 1989, modified 2011]
 
 


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