Malate dehydrogenase (NADP+)

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malate dehydrogenase (NADP+)
Identifiers
EC number1.1.1.82
CAS number37250-19-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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. 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. PMC 1179348. PMID 4395182.