EC 1.3.1.9 - Enoyl-[acyl-carrier-protein] reductase (NADH)

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IntEnz Enzyme Nomenclature
EC 1.3.1.9

Names

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

Reaction

Comments:

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 FAS-I enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004318 , GO:0016631
CAS Registry Number: 37251-08-4
UniProtKB/Swiss-Prot: (148) [show] [UniProt]

References

  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]

[EC 1.3.1.9 created 1972, modified 2013]