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

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+)

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Results	in table
49	Activating Compound
445	AA Sequence
1	Application
1	CAS Registry Number
12	Cloned(Commentary)
27	Cofactor
4	Crystallization (Commentary)
8	Expression
24	General Information
3	General Stability
30	Inhibitors
125	KM Value [mM]
39	Localization
3	Metals/Ions
41	Molecular Weight [Da]
41	Natural Substrates/ Products (Substrates)
116	Organism
1	Oxidation Stability
10	Pathway
5	PDB ID
13	pH Optimum
1	pH Range
1	pH Stability
1	Posttranslational Modification
38	Protein Variants
14	Purification (Commentary)
2	Reaction
3	Reaction Type
107	Reference
2	Renatured (Commentary)
43	Source Tissue
8	Specific Activity [micromol/min/mg]
1	Storage Stability
139	Substrates and Products (Substrate)
34	Subunits
100	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
2	Temperature Range [°C]
7	Temperature Stability [°C]
12	Turnover Number [1/s]

General Stability

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

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

a small carboxy-terminal peptide of the native enzyme is accessible to proteolytic degradation followed by activation of the inactive oxidized enzyme. This peptide is involved in the regulation of activity, tetramer formation and thioredoxin binding

Pisum sativum

-

287392

denaturation by 2 M guanidine-HCl

Pisum sativum

-

287392

no effect of guanidine/HCl up to 0.25 M on the quarternary structure of the enzyme in its oxidized and reduced form. In the oxidized state the enzyme undergoes guanidine-dependent dissociation to the monomer with a midpoint of transition at 0.5 M. The kinetic of unfolding is significantly faster for the reduced than for the oxidized enzyme

Pisum sativum

-

287389