Enoyl-(acyl-carrier-protein) reductase (NADPH, B-specific)

enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific)
Identifiers
EC no.	1.3.1.10
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

In enzymology, enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) (EC 1.3.1.10) is an enzyme that catalyzes the chemical reaction

The enzyme converts the trans double bond of a thioester attached to an acyl carrier protein to the corresponding saturated compound using nicotinamide adenine dinucleotide phosphate (NADPH) and a proton as reducing agent. ^{[1] [2] [3] [4]}

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

1. Enzyme 1.3.1.10 at KEGG Pathway Database.
2. Saito K, Kawaguchi A, Okuda S, Seyama Y, Yamakawa T (1980). "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. doi:10.1016/0005-2760(80)90026-0. PMID   6990992.
3. Seyama Y, Kasama T, Yamakawa T, Kawaguchi A, Saito K (November 1977). "Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase". J. Biochem. 82 (5). Tokyo: 1325–9. doi: 10.1093/oxfordjournals.jbchem.a131820 . PMID   338601.
4. Weeks G, Wakil SJ (1968). "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. doi: 10.1016/S0021-9258(19)56970-8 . PMID   4384650.