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Acyl-CoA dehydrogenase (NADP+)

Class of enzymes From Wikipedia, the free encyclopedia

In enzymology, acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction

RCH2CH2CO-CoA + NADP+ RCH2=CH2CO-CoA + NADPH + H+
Rendering of Crotonyl CoA Carboxylase/Reductase, an oxidoreductase
Structure of Crotonyl CoA carboxylase/reductase. From Streptomycs collinus.[1]

The two substrates of this enzyme are an acyl-CoA and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are the corresponding 2,3-dehydroacyl-CoA, reduced NADPH, and a proton. The enzyme does not alter the length of the chain attached to coenzyme A but creates a double bond adjacent to the carbonyl group.[2][3][4]

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+).

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