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.

Reaction

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

Synonyms

(S)-malate dehydrogenase, dehydrogenase, malate (nicotinamide adenine dinucleotide phosphate), malate NADP dehydrogenase, malic dehydrogenase (nicotinamide adenine dinucleotide phosphate), MDH, NADP 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+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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