Acyl-CoA dehydrogenase (NADP+)
class of enzymes
In enzymology, acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction
RCH2CH2CO-CoA + NADP+
⇌
{\displaystyle \rightleftharpoons }
RCH2=CH2CO-CoA + NADPH + H+
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.
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+).
“Acyl-CoA dehydrogenase (NADP+)” enters the record as class of enzymes. Crown Archives preserves that source wording while asking what Acyl-CoA, dehydrogenase and NADP can confirm, complicate or overturn.
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This entry incorporates text from “Acyl-CoA dehydrogenase (NADP+)” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.