| EC |
1.3.1.104 |
| Accepted name: |
enoyl-[acyl-carrier-protein] reductase (NADPH) |
| Reaction: |
an acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+ |
| Other name(s): |
acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl-ACP reductase (ambiguous); fabL (gene name) |
| Systematic name: |
acyl-[acyl-carrier protein]:NADP+ oxidoreductase |
| Comments: |
The 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 the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
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. [DOI] [PMID: 11007778] |
| 2. |
Kim, K.H., Park, J.K., Ha, B.H., Moon, J.H. and Kim, E.E. Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 (2007) 246–248. [DOI] [PMID: 17329825] |
| 3. |
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. [DOI] [PMID: 21185310] |
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| [EC 1.3.1.104 created 2013] |
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