Acyl-CoA dehydrogenase (NADP+)
| acyl-CoA dehydrogenase (NADP+) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.1.8 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction
- acyl-CoA + NADP+ 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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1YXM.
References
[edit]- ^ 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.; rendered using PyMOL.
- Dommes V, Luster W, Cvetanovic M, Kunau WH (1982). "Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli". Eur. J. Biochem. 125 (2): 335–41. doi:10.1111/j.1432-1033.1982.tb06688.x. PMID 6749495.
- Seubert W, Lamberts I, Kramer R, Ohly B (1968). "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. doi:10.1016/0005-2760(68)90180-x. PMID 4387390.
