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3-oxoacyl-(acyl-carrier-protein) reductase

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Enzyme
3-oxoacyl- reductase
3-oxoacyl- reductase homotetramer, Vibrio cholerae
Identifiers
EC no.1.1.1.100
CAS no.37250-34-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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In enzymology, a 3-oxoacyl- reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction

3-oxoacyl-(ACP) + NADPH + H {\displaystyle \rightleftharpoons } (3R)-3-hydroxyacyl-(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-:NADP oxidoreductase. Other names in common use include beta-ketoacyl-(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-reductase, and 3-oxoacyl-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- reductase, beta-hydroxyacyl- dehydrase, and enoyl- 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.
Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor
1.1.2: cytochrome acceptor
1.1.3: oxygen acceptor
1.1.4: disulfide as acceptor
1.1.5: quinone/similar acceptor
1.1.99: other acceptors
Metabolism: lipid metabolism / fatty acid metabolism, triglyceride and fatty acid enzymes
Synthesis
Malonyl-CoA synthesis
Fatty acid synthesis/
Fatty acid synthase
Fatty acid desaturases
Triacyl glycerol
Degradation
Acyl transport
Beta oxidation
General
Unsaturated
Odd chain
Other
To acetyl-CoA
Aldehydes
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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