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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.3.1.10/1.3.1.39/2.3.1.85/2.3.1.86

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: 1.3.1.10 , 1.3.1.39 , 2.3.1.85 , 2.3.1.86

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

In Pathway: palmitate biosynthesis I (animals and fungi)

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

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.

Direct generic reaction:
a 2,3,4-saturated fatty acyl-[acp] + NADP+ ← a trans-2-enoyl-[acyl-carrier protein] + NADPH + H+ (1.3.1.10/1.3.1.39/1.3.1.104/2.3.1.85/2.3.1.86)

Enzyme Commission Primary Name for 1.3.1.10: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

Enzyme Commission Synonyms for 1.3.1.10: acyl-ACP dehydrogenase (ambiguous), enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase, NADPH 2-enoyl Co A reductase, enoyl acyl-carrier-protein reductase (ambiguous), enoyl-ACP reductase (ambiguous), acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific), acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific), enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)

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 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 1.3.1.10:
One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase, an enzyme found in yeasts (Ascomycota and the Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH).

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 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: [Seyama77, Dugan70, CarlisleMoore05, Heath00, Kim11d, Stoops79, Wakil83, Schweizer73, Tehlivets07]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.3.1.10 , BRENDA:EC:1.3.1.39 , BRENDA:EC:2.3.1.85 , BRENDA:EC:2.3.1.86 , ENZYME:EC:1.3.1.10 , ENZYME:EC:1.3.1.39 , ENZYME:EC:2.3.1.85 , ENZYME:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:1.3.1.10 , IUBMB-ExplorEnz:EC:1.3.1.39 , IUBMB-ExplorEnz:EC:2.3.1.85 , IUBMB-ExplorEnz:EC:2.3.1.86


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

Heath00: 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

Kim11d: 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

Seyama77: Seyama Y, Kasama T, Yamakawa T, Kawaguchi A, Saito K (1977). "Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase." J Biochem 82(5);1325-9. PMID: 338601

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 18.5 on Sun Nov 23, 2014, BIOCYC13B.