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Malate dehydrogenase (NADP+)
Enzyme class From Wikipedia, the free encyclopedia
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In enzymology, malate dehydrogenase (NADP+) (EC 1.1.1.82) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are (S)-malic acid and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are oxaloacetic acid, NADPH, and a proton.[1][2][3][4]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-malate:NADP+ oxidoreductase. Other names in common use include NADP+-malic enzyme, NADP+-malate dehydrogenase, malic dehydrogenase (nicotinamide adenine dinucleotide phosphate), malate NADP+ dehydrogenase, NADP+ malate dehydrogenase, NADP+-linked malate dehydrogenase, and malate dehydrogenase (NADP+). This enzyme participates in pyruvate metabolism and carbon fixation. This enzyme has at least one effector, hn.
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Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1CIV and 7MDH.
References
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