1.1.1.37: malate dehydrogenase

This is an abbreviated version, for detailed information about malate dehydrogenase, go to the full flat file.

Reaction

(S)-malate
+
NAD+
=
oxaloacetate
+
NADH
+
H+

Synonyms

(R)-2-hydroxyacid dehydrogenase, (S)-malate dehydrogenase, CaMDH, cMDH, cMDH -S, cMDH-L, cyMDH, cytosolic malate dehydrogenase, cytosolic MDH, cytosolic NAD-dependent malate dehydrogenase, halophilic malate dehydrogenase, HmMalDH, L-malate dehydrogenase, L-malate-NAD oxidoreductase, L-malate: NAD oxidoreductase, L-malate: NAD+ oxidoreductase, L-malate:NAD-oxidoreductase, L-MDH, m-MDH, malate (NAD) dehydrogenase, malate dehydrogenase, malate dehydrogenase (NAD), malate dehydrogenase 1, malate dehydrogenase 2, malate: NAD oxidoreductase, MalDH, malic acid dehydrogenase, malic dehydrogenase, mbNAD-MDH, MDH, MDH A, MDH B1, MDH B2, Mdh1, MDH2, Mdh2a, Mdh2b, mitochondrial malate dehydrogenase, mitochondrial MDH, mMDH, mNAD-MDH, More, NAD+-dependent malate dehydrogenase, NAD+-dependent MDH, NAD+-MDH enzymes, NAD-dependent malate dehydrogenase, NAD-dependent malic dehydrogenase, NAD-dependent MDH, NAD-L-malate dehydrogenase, NAD-linked malate dehydrogenase, NAD-malate dehydrogenase, NAD-malic dehydrogenase, NAD-MDH, NAD-specific malate dehydrogenase, Pcal_1699, peroxisomal NAD+-malate dehydrogenase 1, peroxisomal NAD+-malate dehydrogenase 2, PMDH, PMDH1, PMDH2, regulatory subunit of nucleic acid-conducting channel, s-MDH, SrMalDH, TaMDH, VEG69, Vegetative protein 69, YlMdh2p, [LDH-like] MDH

ECTree

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

Crystallization

Crystallization on EC 1.1.1.37 - malate dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop method, crystal structure in complex with NAD+ solved at 2.9 A resolution. Crystal structure shows a compact homodimer with one coenzyme bound per subunit
-
s-MDH
-
hanging drop vapour-diffusion method
s-MDH
-
hanging drop vapour diffusion method, using 100 mM N-(2-acetamido)-iminodiacetic acid pH 6.5, 0.2 M sodium acetate, 30% (w/v) PEG MME 5000, 5% (v/v) glycerol
tetrameric enzyme, hanging drop vapour diffusion method, 15C, 17 mg/ml protein in 10 mM potassium phosphate buffer, pH 7.0, equilibration of the 0.002 ml protein drop against 500 ml reservoir solution consisting of 1.4 M ammonium sulfate, 5% v/v MPD, 2 mM NAD+, 50 mM sodium citrate buffer, pH 5.5, 2-3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution
sitting drop reverse vapour diffusion method, crystal structure of the R207S/R292S mutant of malate dehydrogenase is solved at 1.95 A
-
the structure of the mutant E267R apoenzyme is determined to 2.6 A resolution and the structure of the wild-type apoenzyme is determined to 2.9 A resolution
-
s-MDH
-
; in presence of ethylene glycol 4000
-
crystals of space groups P321, P3121 or P3,21, resolution to 5 A
-
cytoplasmic enzyme
-
recombinant porcine cMDH
-
crystals of space group P21, resolution to 4 A
-
mutant EX7 (with altered coenzyme specificity from NADH towards NADPH) in complex with NADPH or NADH, 2.0 A resolution