Malate dehydrogenase (NADP+)
malate dehydrogenase (NADP+) | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.82 | ||||||||
CAS no. | 37250-19-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a malate dehydrogenase (NADP+) (EC 1.1.1.82) is an enzyme that catalyzes the chemical reaction
- (S)-malate + NADP+ oxaloacetate + NADPH + H+
Thus, the two substrates of this enzyme are (S)-malate and NADP+, whereas its 3 products are oxaloacetate, NADPH, and H+.
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.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1CIV and 7MDH.
References
[edit]- Connelly JL, Danner DJ, Bowden JA (1968). "Branched chain alpha-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid dehydrogenase". J. Biol. Chem. 243 (6): 1198–203. doi:10.1016/S0021-9258(19)56972-1. PMID 5689906.
- Johnson HS (1971). "NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis". Biochem. Biophys. Res. Commun. 43 (4): 703–9. doi:10.1016/0006-291X(71)90672-3. PMID 4397919.
- Johnson HS, Hatch MD (1970). "Properties and regulation of leaf nicotinamide–adenine dinucleotide phosphate–malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis". Biochem. J. 119 (2): 273–80. doi:10.1042/bj1190273. PMC 1179348. PMID 4395182.