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1.1.1.82: malate dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about malate dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.1.1.82

Reaction

(S)-malate
+
NADP+
=
oxaloacetate
 +
NADPH
 +
H+

Synonyms

(S)-malate dehydrogenase, dehydrogenase, malate (nicotinamide adenine dinucleotide phosphate), L-malate:NAD oxidoreductase, malate NADP dehydrogenase, malic dehydrogenase (nicotinamide adenine dinucleotide phosphate), MDH, NADP malate dehydrogenase, NADP+-dependent malate dehydrogenase, NADP-dependent malate dehydrogenase, NADP-linked malate dehydrogenase, NADP-malate dehydrogenase, NADP-malic enzyme, NADP-MDH, NADP-MDH1, NADP-MDH2, NADPH-MDH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.82 malate dehydrogenase (NADP+)

Temperature Stability

Temperature Stability on EC 1.1.1.82 - malate dehydrogenase (NADP+)

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
purified recombinant enzyme, 10 min, stable. The hyperthermostability of the Aeropyrum pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme
37
-
pH 8.0, 10 min, reduced enzyme without NADPH, about 50% loss of activity
55
-
pH 8.0, 10 min, oxidized enzyme without NADPH, about 75% loss of activity
60
-
pH 8.0, 10 min, oxidized enzyme in presence of NADPH, about 50% loss of activity
90
purified recombinant enzyme, 10 min, stable. The hyperthermostability of the Aeropyrum pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme