Metabolic Modeling Tutorial
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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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.3.1.9

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: 1.3.1.9

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

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 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] + 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): 34.414032 Inferred 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 [Yu11]. 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: ?

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

Yu11: 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 SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, biocyc13.