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| [[image:3HZZ_cartoonpic.png|thumb|upright|alt = Rendering of Crotonyl CoA Carboxylase/Reductase, an oxidoreductase|'''Structure of Crotonyl CoA carboxylase/reductase'''. From ''Streptomycs collinus''.<ref name="Scarsdale10">{{PDB|3HZZ}}; {{cite journal | author = Scarsdale, J.N., Musayev, F.N., Hazzard, C., Florova, G., Reynolds, K., Wright, H.T.| title = Structure of Streptomycs collinus crotonyl COA carboxylase/reductase | journal = To be Published | year = 2010 | doi = 10.2210/pdb3hzz/pdb | url = http://www.rcsb.org/pdb/explore/explore.do?structureId=3HZZ}}; rendered using [http://pymol.sourceforge.net PyMOL]. </ref>]]
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| {{enzyme
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| | Name = acyl-CoA dehydrogenase (NADP+)
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| | EC_number = 1.3.1.8
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| | CAS_number = 37251-07-3
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| | IUBMB_EC_number = 1/3/1/8
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| | GO_code = 0047616
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| }}
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| In [[enzymology]], an '''acyl-CoA dehydrogenase (NADP+)''' ({{EC number|1.3.1.8}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :acyl-CoA + NADP<sup>+</sup> <math>\rightleftharpoons</math> 2,3-dehydroacyl-CoA + NADPH + H<sup>+</sup>
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[acyl-CoA]] and [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[2,3-dehydroacyl-CoA]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], and [[hydrogen ion|H<sup>+</sup>]].
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| This enzyme belongs to the family of [[oxidoreductase]]s, 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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| ==Structural studies==
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| As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|1YXM}}.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Dommes V, Luster W, Cvetanovic M, Kunau WH | date = 1982 | title = Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli | journal = Eur. J. Biochem. | volume = 125 | pages = 335–41 | pmid = 6749495 | doi = 10.1111/j.1432-1033.1982.tb06688.x | issue = 2 }}
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| * {{cite journal | author = Seubert W, Lamberts I, Kramer R, Ohly B | date = 1968 | title = On the mechanism of malonyl-CoA-independent fatty acid synthesis. I The mechanism of elongation of long-chain fatty acids by acetyl-CoA | journal = Biochim. Biophys. Acta. | volume = 164 | pages = 498–517 | pmid = 4387390 | issue = 3 }}
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| {{1.3-enzyme-stub}}
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| [[Category:EC 1.3.1]]
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| [[Category:NADPH-dependent enzymes]]
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| [[Category:Enzymes of known structure]]
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