EC - Enoyl-[acyl-carrier-protein] reductase (NADH)

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IntEnz Enzyme Nomenclature


Accepted name:
enoyl-[acyl-carrier-protein] reductase (NADH)
Other names:
NADH-enoyl acyl carrier protein reductase
NADH-specific enoyl-ACP reductase
enoyl-ACP reductase
enoyl-[acyl carrier protein] reductase
acyl-[acyl-carrier-protein]:NAD+ oxidoreductase
fabI (gene name)
inhA (gene name)
Systematic name:
acyl-[acyl-carrier protein]:NAD+ oxidoreductase



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 [3]. The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons [4,5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004318
CAS Registry Number: 37251-08-4
UniProtKB/Swiss-Prot: (143) [show] [UniProt]


  1. Shimakata, T. and Stumpf, P.K.
    Purification and characterizations of β-ketoacyl-[acyl-carrier-protein] reductase, β-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves.
    Arch. Biochem. Biophys. 218: 77-91 (1982). [PMID: 6756317]
  2. Weeks, G. and Wakil, S.J.
    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. 243: 1180-1189 (1968). [PMID: 4384650]
  3. Yu, X., Liu, T., Zhu, F., Khosla, C.
    In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli.
    Proc. Natl. Acad. Sci. U.S.A. 108: 18643-18648 (2011). [PMID: 22042840]
  4. Quemard, A., Sacchettini, J. C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W. R., Blanchard, J. S.
    Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis.
    Biochemistry 34: 8235-8241 (1995). [PMID: 7599116]
  5. Rozwarski, D. A., Vilcheze, C., Sugantino, M., Bittman, R., Sacchettini, J. C.
    Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.
    J. Biol. Chem. 274: 15582-15589 (1999). [PMID: 10336454]

[EC created 1972, modified 2013]