twitter

MetaCyc Reaction: 1.3.1.39/1.3.1.104/2.3.1.85/2.3.1.86

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 1.3.1.39 , 1.3.1.104 , 2.3.1.85 , 2.3.1.86

Enzymes and Genes:

Bacillus subtilis subtilis 168 : enoyl-[acyl-carrier-protein] reductase (NADPH) Inferred from experiment : fabL
Homo sapiens : fatty acid synthase Inferred from experiment : FASN
Saccharomyces cerevisiae : fatty acid synthase, β subunit : FAS1

In Pathway: fatty acid elongation -- saturated

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Instance reactions:
a hexanoyl-[acyl-carrier-protein] + NADP+ ← a trans hex-2-enoyl-[acp] + NADPH + H+ (1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86)

a myristoyl-[acp] + NADP+ ← a trans tetradec-2-enoyl-[acp] + NADPH + H+ (1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86)

a palmitoyl-[acp] + NADP+ ← a trans hexadecenoyl-[acp] + NADPH + H+ (1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86)

a stearoyl-[acp] + NADP+ ← a trans-octadec-2-enoyl-[acp] + NADPH + H+ (1.3.1.10/2.3.1.86)

a dodecanoyl-[acp] + NADP+ ← a trans dodec-2-enoyl-[acp] + NADPH + H+ (1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86)

an octanoyl-[acp] + NADP+ ← a trans oct-2-enoyl-[acp] + NADPH + H+ (1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86)

a decanoyl-[acp] + NADP+ ← a trans2-decenoyl-[acp] + NADPH + H+ (1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86)

Enzyme Commission Primary Name for 1.3.1.39: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

Enzyme Commission Synonyms for 1.3.1.39: acyl-ACP dehydrogenase, enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, NADPH 2-enoyl Co A reductase, enoyl-ACp reductase, enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific), acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific), enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific), acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)

Enzyme Commission Primary Name for 1.3.1.104: enoyl-[acyl-carrier-protein] reductase (NADPH)

Enzyme Commission Synonyms for 1.3.1.104: acyl-ACP dehydrogenase (ambiguous), enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, NADPH 2-enoyl Co A reductase, enoyl-ACP reductase (ambiguous), fabL (gene name)

Enzyme Commission Primary Name for 2.3.1.85: fatty-acid synthase

Enzyme Commission Synonyms for 2.3.1.85: FASN (gene name)

Enzyme Commission Primary Name for 2.3.1.86: fatty-acyl-CoA synthase

Enzyme Commission Synonyms for 2.3.1.86: yeast fatty acid synthase, FAS1 (gene name), FAS2 (gene name)

Standard Gibbs Free Energy (ΔrG in kcal/mol): 33.16577 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 1.3.1.39:
This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is also one of the activities of animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH) and EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific).

Enzyme Commission Summary for 1.3.1.104:
The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).

Enzyme Commission Summary for 2.3.1.85:
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.

Enzyme Commission Summary for 2.3.1.86:
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxyacyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase. The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.

Citations: [Dugan70, CarlisleMoore05, Heath00a, Kim11c, Kim07e, Stoops79, Wakil83, Schweizer73, Tehlivets07]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:1.3.1.39 , BRENDA:EC:1.3.1.104 , BRENDA:EC:2.3.1.85 , BRENDA:EC:2.3.1.86 , ENZYME:EC:1.3.1.39 , ENZYME:EC:1.3.1.104 , ENZYME:EC:2.3.1.85 , ENZYME:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:1.3.1.39 , IUBMB-ExplorEnz:EC:1.3.1.104 , IUBMB-ExplorEnz:EC:2.3.1.85 , IUBMB-ExplorEnz:EC:2.3.1.86 , UniProt:RELATED-TO:P12276 , UniProt:RELATED-TO:P12785 , UniProt:RELATED-TO:P49327

Credits:
Revised 12-Dec-2011 by Caspi R , SRI International


References

CarlisleMoore05: Carlisle-Moore L, Gordon CR, Machutta CA, Miller WT, Tonge PJ (2005). "Substrate recognition by the human fatty-acid synthase." J Biol Chem 280(52);42612-8. PMID: 16215233

Dugan70: Dugan RE, Slakey LL, Porter JW (1970). "Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis." J Biol Chem 245(23);6312-6. PMID: 4394955

Heath00a: Heath RJ, Su N, Murphy CK, Rock CO (2000). "The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis." J Biol Chem 275(51);40128-33. PMID: 11007778

Kim07e: Kim KH, Park JK, Ha BH, Moon JH, Kim EE (2007). "Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis." Acta Crystallogr Sect F Struct Biol Cryst Commun 63(Pt 3);246-8. PMID: 17329825

Kim11c: Kim KH, Ha BH, Kim SJ, Hong SK, Hwang KY, Kim EE (2011). "Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis." J Mol Biol 406(3);403-15. PMID: 21185310

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Schweizer73: Schweizer E, Kniep B, Castorph H, Holzner U (1973). "Pantetheine-free mutants of the yeast fatty-acid-synthetase complex." Eur J Biochem 39(2);353-62. PMID: 4590449

Stoops79: Stoops JK, Ross P, Arslanian MJ, Aune KC, Wakil SJ, Oliver RM (1979). "Physicochemical studies of the rat liver and adipose fatty acid synthetases." J Biol Chem 254(15);7418-26. PMID: 457689

Tehlivets07: Tehlivets O, Scheuringer K, Kohlwein SD (2007). "Fatty acid synthesis and elongation in yeast." Biochim Biophys Acta 1771(3);255-70. PMID: 16950653

Wakil83: Wakil SJ, Stoops JK, Joshi VC (1983). "Fatty acid synthesis and its regulation." Annu Rev Biochem 52;537-79. PMID: 6137188


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sun Apr 26, 2015, biocyc14.