Biology:Enoyl-(acyl-carrier-protein) reductase (NADPH, B-specific)
| enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.3.1.10 | ||||||||
| CAS number | 37251-09-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10) is an enzyme that catalyzes the chemical reaction
- acyl-[acyl-carrier-protein] + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH + H+
Thus, the two substrates of this enzyme are acyl-[acyl-carrier-protein] and NADP+, whereas its 3 products are trans-2,3-dehydroacyl-[acyl-carrier-protein], NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific). Other names in common use include acyl-ACP dehydrogenase, reductase, enoyl-[acyl carrier protein] (reduced nicotinamide, adenine dinucleotide phosphate), NADPH 2-enoyl Co A reductase, enoyl acyl-carrier-protein reductase, enoyl-ACP reductase, and enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). This enzyme participates in fatty acid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ULU and 2YW9.
References
- "Incorporation of hydrogen atoms from deuterated water and stereospecifically deuterium-labeled nicotin amide nucleotides into fatty acids with the Escherichia coli fatty acid synthetase system". Biochim. Biophys. Acta 618 (2): 202–13. 1980. doi:10.1016/0005-2760(80)90026-0. PMID 6990992.
- "Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase". J. Biochem. (Tokyo) 82 (5): 1325–9. November 1977. doi:10.1093/oxfordjournals.jbchem.a131820. PMID 338601.
- "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 (6): 1180–9. 1968. PMID 4384650.
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