Acyl-CoA dehydrogenase (NADP+) explained

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+)
Ec Number:	1.3.1.8
Cas Number:	37251-07-3
Go Code:	0047616

In enzymology, an acyl-CoA dehydrogenase (NADP+) is an enzyme that catalyzes the chemical reaction

acyl-CoA + NADP⁺

\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 .

References

• 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 . 335 - 41 . 6749495 . 10.1111/j.1432-1033.1982.tb06688.x . 2 .
• 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 . 498 - 517 . 4387390 . 3 . 10.1016/0005-2760(68)90180-x.

Notes and References

1. Scarsdale, J.N. . Musayev, F.N. . Hazzard, C. . Florova, G. . Reynolds, K. . Wright, H.T.. Structure of Streptomycs collinus crotonyl COA carboxylase/reductase . Worldwide Protein Data Bank . 2010 . 10.2210/pdb3hzz/pdb . ; rendered using PyMOL.