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MetaCyc Reaction: 1.3.1.9

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number: 1.3.1.9

Enzymes and Genes:

Brassica napus: enoyl-[acyl-carrier-protein] reductase [NADH], chloroplasticInferred from experiment: enrA1
Escherichia coli K-12 substr. MG1655: enoyl-[acyl-carrier-protein] reductaseInferred from experiment: fabI
Mycobacterium tuberculosis H37Rv: fatty acid synthaseInferred by computational analysis: fas
Streptococcus pneumoniae: enoyl-[acyl-carrier-protein] reductase (NADH): fabK
Vibrio albensis: enoyl-[acyl-carrier-protein] reductase (NADH): fabV

In Pathway: palmitate biosynthesis II (bacteria and plants)

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

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Direct generic reactions:
a 2,3,4-saturated fatty acyl-[acp] + NAD+ ← a trans-2-enoyl-[acyl-carrier protein] + NADH + H+ (1.3.1.M3)

a 2,3,4-saturated fatty acyl-[acp] + NAD+ ← a trans-2-enoyl-[acyl-carrier protein] + NADH + H+ (1.3.1.9)

Enzyme Commission Primary Name: enoyl-[acyl-carrier-protein] reductase (NADH)

Enzyme Commission Synonyms: enoyl-[acyl carrier protein] reductase, enoyl-ACP reductase, NADH-enoyl acyl carrier protein reductase, NADH-specific enoyl-ACP reductase, acyl-[acyl-carrier-protein]:NAD+ oxidoreductase, fabI (gene name), inhA (gene name)

Standard Gibbs Free Energy (ΔrG in kcal/mol): 34.414032Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme catalyses an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier-protein] derivatives of the elongating fatty acid moiety. The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18 [Yu11a]. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12-24 carbons [Quemard95, Rozwarski99].

Citations: [Shimakata82, Weeks68]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:1.3.1.9, ENZYME:EC:1.3.1.9, IUBMB-ExplorEnz:EC:1.3.1.9


References

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

Quemard95: Quemard A, Sacchettini JC, Dessen A, Vilcheze C, Bittman R, Jacobs WR, Blanchard JS (1995). "Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis." Biochemistry 34(26);8235-41. PMID: 7599116

Rozwarski99: Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC (1999). "Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate." J Biol Chem 274(22);15582-9. PMID: 10336454

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

Weeks68: Weeks G, Wakil SJ (1968). "Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli." J Biol Chem 1968;243(6);1180-9. PMID: 4384650

Yu11a: Yu X, Liu T, Zhu F, Khosla C (2011). "In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli." Proc Natl Acad Sci U S A 108(46);18643-8. PMID: 22042840


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 Pathway Tools version 19.5 (software by SRI International) on Wed May 4, 2016, biocyc14.