EC 1 - Oxidoreductases
EC 1.3 - Acting on the CH-CH group of donors
EC 1.3.1 - With NAD+ or NADP+ as acceptor
EC 1.3.1.9 - Enoyl-[acyl-carrier-protein] reductase (NADH)
IntEnz view
ENZYME view
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)
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
- an acyl-acyl-carrier protein + NAD+ = a trans-2,3-dehydroacyl-acyl-carrier protein + NADH + H+
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
Gene Ontology:
GO:0004318
,
GO:0016631
CAS Registry Number:
37251-08-4
References
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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]
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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]
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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]