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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.1.1.100/2.3.1.85/2.3.1.86

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: 1.1.1.100 , 2.3.1.85 , 2.3.1.86

Enzymes and Genes:
fatty acid synthase Inferred by computational analysis : fas ( Mycobacterium tuberculosis H37Rv )
fatty acid synthase : FASN ( Homo sapiens )
fatty acid synthase, α subunit : FAS2 ( Saccharomyces cerevisiae )
3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic Inferred from experiment : AT1G24360 ( Arabidopsis thaliana col )
NADPH-dependent β-ketoacyl reductase : rhlG ( Pseudomonas aeruginosa )
3-oxoacyl-[acyl-carrier-protein] reductase : fabG ( Escherichia coli K-12 substr. MG1655 )

In Pathway: palmitate biosynthesis II (bacteria and plants) , 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 (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ ← a 3-oxoacyl-[acp] + NADPH + H+ (1.1.1.100/2.3.1.85/2.3.1.86)

Enzyme Commission Primary Name for 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase

Enzyme Commission Synonyms for 1.1.1.100: β-ketoacyl-[acyl-carrier protein](ACP) reductase, β-ketoacyl acyl carrier protein (ACP) reductase, β-ketoacyl reductase, β-ketoacyl thioester reductase, β-ketoacyl-ACP reductase, β-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, 3-oxoacyl-[ACP]reductase, (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase

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): 20.375793 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 1.1.1.100:
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.

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: [Prescott72, Shimakata82, Toomey66, Stoops79, Wakil83, Schweizer73, Tehlivets07]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.1.1.100 , BRENDA:EC:2.3.1.85 , BRENDA:EC:2.3.1.86 , ENZYME:EC:1.1.1.100 , ENZYME:EC:2.3.1.85 , ENZYME:EC:2.3.1.86 , IUBMB-ExplorEnz:EC:1.1.1.100 , IUBMB-ExplorEnz:EC:2.3.1.85 , IUBMB-ExplorEnz:EC:2.3.1.86


References

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

Prescott72: Prescott DJ, Vagelos PR (1972). "Acyl carrier protein." Adv Enzymol Relat Areas Mol Biol 36;269-311. PMID: 4561013

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

Shimakata82: Shimakata T, Stumpf PK (1982). "Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acyl-carrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves." Arch Biochem Biophys 218(1);77-91. PMID: 6756317

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

Toomey66: Toomey RE, Wakil SJ (1966). "Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli." Biochim Biophys Acta 116(2);189-97. PMID: 4381013

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 Wed Nov 26, 2014, biocyc14.