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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 ${\displaystyle \rightleftharpoons }$ 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

1. 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.

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