Biology:Acyl-CoA dehydrogenase (NADP+)
thumb|upright|alt=Rendering of Crotonyl CoA Carboxylase/Reductase, an oxidoreductase|Structure of Crotonyl CoA carboxylase/reductase. From Streptomycs collinus.[1]
| acyl-CoA dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.3.1.8 | ||||||||
| CAS number | 37251-07-3 | ||||||||
| 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 | ||||||||
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In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction
- acyl-CoA + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] 2,3-dehydroacyl-CoA + NADPH + H+
Thus, the two substrates of this enzyme are acyl-CoA and NADP+, whereas its 3 products are 2,3-dehydroacyl-CoA, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is acyl-CoA:NADP+ 2-oxidoreductase. Other names in common use include 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide, phosphate), enoyl coenzyme A reductase, crotonyl coenzyme A reductase, crotonyl-CoA reductase, and acyl-CoA dehydrogenase (NADP+).
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YXM.
References
- ↑ PDB: 3HZZ; Scarsdale, J.N.; Musayev, F.N.; Hazzard, C.; Florova, G.; Reynolds, K.; Wright, H.T. (2010). "Structure of Streptomycs collinus crotonyl COA carboxylase/reductase". Worldwide Protein Data Bank. doi:10.2210/pdb3hzz/pdb. http://www.rcsb.org/pdb/explore/explore.do?structureId=3HZZ.; rendered using PyMOL.
- "Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli". Eur. J. Biochem. 125 (2): 335–41. 1982. doi:10.1111/j.1432-1033.1982.tb06688.x. PMID 6749495.
- "On the mechanism of malonyl-CoA-independent fatty acid synthesis. I The mechanism of elongation of long-chain fatty acids by acetyl-CoA". Biochim. Biophys. Acta 164 (3): 498–517. 1968. doi:10.1016/0005-2760(68)90180-x. PMID 4387390.
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