3-oxoacyl-(acyl-carrier-protein) reductase
| 3-oxoacyl-[acyl-carrier-protein] reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3-oxoacyl-[acyl-carrier-protein] reductase homotetramer, Vibrio cholerae | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.100 | ||||||||
| CAS no. | 37250-34-3 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction
- 3-oxoacyl-[acyl-carrier-protein](ACP) + NADPH + H+ (3R)-3-hydroxyacyl-[acyl-carrier-protein](ACP) + NADP+
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group as hydride donor with NAD+ or NADP+ as hydride acceptor. The systematic name of this enzyme class is (3R)-3-hydroxyacyl-[acyl-carrier-protein]:NADP+ oxidoreductase. Other names in common use include beta-ketoacyl-[acyl-carrier protein](ACP) reductase, beta-ketoacyl acyl carrier protein (ACP) reductase, beta-ketoacyl reductase, beta-ketoacyl thioester reductase, beta-ketoacyl-ACP reductase, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl acyl carrier protein reductase, 3-ketoacyl ACP reductase, NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase, and 3-oxoacyl-[ACP]reductase. This enzyme participates in fatty acid biosynthesis and polyunsaturated fatty acid biosynthesis.
Structural studies
As of late 2007, 21 structures have been solved for this class of enzymes, with PDB accession codes 1I01, 1O5I, 1Q7B, 1Q7C, 1ULS, 1UZL, 1UZM, 1UZN, 2A4K, 2B4Q, 2C07, 2FR0, 2FR1, 2NM0, 2NTN, 2P68, 2PFF, 2PH3, 2PNF, 2UVD, and 2Z5L.
References
- Prescott DJ, Vagelos PR (1972). "Acyl Carrier Protein". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 36. pp. 269–311. doi:10.1002/9780470122815.ch8. ISBN 9780470122815. PMID 4561013.
- Shimakata T, Stumpf PK (1982). "Purification and characterizations of beta-Ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves". Arch. Biochem. Biophys. 218 (1): 77–91. doi:10.1016/0003-9861(82)90323-X. PMID 6756317.
- Toomey RE, Wakil SJ (1966). "Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli". Biochim. Biophys. Acta. 116 (2): 189–97. doi:10.1016/0005-2760(66)90001-4. PMID 4381013.
