IUBMB Enzyme Nomenclature


Accepted name: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

Reaction: an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+

Other name(s): acyl-ACP dehydrogenase; enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACp reductase; enoyl-[acyl-carrier-protein] reductase (NADPH2, A-specific); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (A-specific); fabL (gene name); enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (A-specific)

Systematic name: acyl-[acyl-carrier protein]:NADP+ oxidoreductase (Re-specific)

Comments: This enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to an acyl-carrier protein. It is also one of the activities of EC, animal fatty-acid synthase. The mammalian enzyme is Re-specific with respect to NADP+. cf. EC, enoyl-[acyl-carrier-protein] reductase (NADH) and EC, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:


1. Dugan, R.E., Slakey, L.L. and Porter, L.W. Stereospecificity of the transfer of hydrogen from reduced nicotinamide adenine dinucleotide phosphate to the acyl chain in the dehydrogenase-catalyzed reactions of fatty acid synthesis. J. Biol. Chem. 245 (1970) 6312-6316. [PMID: 4394955]

2. Carlisle-Moore, L., Gordon, C.R., Machutta, C.A., Miller, W.T. and Tonge, P.J. Substrate recognition by the human fatty-acid synthase. J. Biol. Chem. 280 (2005) 42612-42618. [PMID: 16215233]

3. Heath, R.J., Su, N., Murphy, C.K. and Rock, C.O. The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J. Biol. Chem. 275 (2000) 40128-40133. [PMID: 11007778]

4. Kim, K.H., Ha, B.H., Kim, S.J., Hong, S.K., Hwang, K.Y. and Kim, E.E. Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis. J. Mol. Biol. 406 (2011) 403-415. [PMID: 21185310]

[EC created 1986, modified 2013]

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