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Escherichia coli K-12 substr. MG1655 Reaction:

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

EC Number:

Enzymes and Genes:
enoyl-[acyl-carrier-protein] reductaseInferred from experiment: fabI

In Pathway: palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate)

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.

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)

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

Gene-Reaction Schematic

Instance reactions of [an acyl-[acyl-carrier protein] + NAD+ = a trans-2-enoyl-[acyl-carrier protein] + NADH + H+] (
i1: a dodecanoyl-[acp] + NAD+ ← a (2E)-dodec-2-enoyl-[acp] + NADH + H+ (

i2: a palmitoyl-[acp] + NAD+ ← a trans hexadecenoyl-[acp] + NADH + H+ (

i3: a myristoyl-[acp] + NAD+ ← a trans tetradec-2-enoyl-[acp] + NADH + H+ (

i4: a butyryl-[acp] + NAD+ ← a crotonyl-[acp] + NADH + H+ (

i5: a decanoyl-[acp] + NAD+ ← a (2E)-dec-2-enoyl-[acp] + NADH + H+ (

i6: a hexanoyl-[acyl-carrier-protein] + NAD+ ← a trans hex-2-enoyl-[acp] + NADH + H+ (

i7: an octanoyl-[acp] + NAD+ ← a trans oct-2-enoyl-[acp] + NADH + H+ (

i8: a cis-vaccenoyl-[acp] + NAD+ ← a (2-trans-11-cis)-vaccen-2-enoyl-[acp] + NADH + H+ (

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


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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc13.