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1.1.1.37: malate dehydrogenase

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

Word Map on EC 1.1.1.37

Reaction

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

Synonyms

(R)-2-hydroxyacid dehydrogenase, (S)-malate dehydrogenase, A8B73_11505, CaMDH, cMDH, cMDH -S, cMDH-L, cyMDH, cyMDH1, cyMDH2, cyMDH3, cytMDH, cytMDH1, cytosolic malate dehydrogenase, cytosolic malate dehydrogenase 1, cytosolic MDH, cytosolic NAD-dependent malate dehydrogenase, flo16, floury endosperm16, halophilic malate dehydrogenase, HmMalDH, L-malate dehydrogenase, L-malate dehydrogenases, L-malate-NAD oxidoreductase, L-malate-NAD-oxidoreductase, L-malate: NAD oxidoreductase, L-malate: NAD+ oxidoreductase, L-malate:NAD oxidoreductase, L-malate:NAD-oxidoreductase, L-MDH, LDH-like malate dehydrogenase, ldh0076, LEUM_0076, 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, Mdh3, mitochondrial malate dehydrogenase, mitochondrial MDH, mMDH, mNAD-MDH, More, NAD+ malate dehydrogenase, NAD+-dependent malate dehydrogenase, NAD+-dependent MDH, NAD+-MDH enzymes, NAD-dependent cytosolic malate dehydrogenase, NAD-dependent malate dehydrogenase, NAD-dependent MalDH, 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, NADP+-dependent malate dehydrogenase, Pcal_1699, pdNAD-MDH, peroxisomal malate dehydrogenase, peroxisomal NAD+-malate dehydrogenase 1, peroxisomal NAD+-malate dehydrogenase 2, plastid-localized NAD-dependent MDH, plastidial NAD+-dependent malate dehydrogenase, plastidial NAD-dependent malate dehydrogenase, plastidial NAD-dependent malate dehydrogenase 1, plNAD-MDH, 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
hanging drop vapor diffusion method, using 0.18 M ammonium sulfate, 0.09 M sodium acetate trihydrate, pH 4.6, 27% (w/v) polyethylene glycol monomethyl ether 2000, and 10% (v/v) glycerol
purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of 0.0003 ml 6 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 200 mM NaCl, and 10% glycerol, with 0.0003 ml of reservoir solution containing 1.2 M sodium citrate tribasic dihydrate, pH 7.0, 20°C, method optimization, X-ray diffraction structure determination and analysis
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
-
crystal structure determination and analysis
-
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, 15°C, 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
purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 4 mg/ml protein in 50 mM Tris-HCl, pH 7.2, 50 mM NaCl, and 10 mM Tb-Xo4 crystallophore, with 0.001 ml of reservoir solution containing 10% PEG 6000 and 100 mM HEPES, pH 7.0, at 20°C, X-ray diffraction structure determination and analysis, molecular replacement using the structure of Haloferax volcanii MalDH (PDB ID 4BGU) as search template, modeling
enzyme in complex with NAD+, hanging drop vapor diffusion method, using 35% (v/v) 2-ethoxyethanol and 0.1M sodium cacodylate/hydrochloric acid pH 6.0 at 20°C.Enzyme as ternary complex with malate and NAD+, hanging drop vapor diffusion method, using 40% (w/v) polyethylene glycol 300, 0.1M CHES/sodium hydroxide pH 9.5, and 0.2 M sodium chloride
apo enzyme, a binary complex of enzyme and NAD+, and a ternary complex of enzyme and oxaloacetate with ADP-ribose, sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 25-28% (w/v) PEG400, 180-220 mM CaCl2
s-MDH
-
apoenzyme, sitting drop vapor diffusion method, using 0.1 M CHES pH 9.5, 30% (w/v) PEG 400. Enzyme in complex with NAD+, sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.1 M bis-Tris pH 5.5, 0.2 M MgCl2. Enzyme in complex with NAD+ and oxaloacetate, sitting drop vapor diffusion method, using 20% (w/v) PEG 10000, 0.1 M HEPES pH 7.5
-
crystals of space groups P321, P3121 or P3,21, resolution to 5 A
-
in presence of ethylene glycol 4000
-
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
purified recombinant enzyme in apoform and in complex with NAD+, sitting drop vapor diffusion method, mixing 500 nl of 10 mg/ml protein with an equal volume of mother liquor and equilibration against 0.1 ml of the crystallization solution containing 100 mM Tris-HCl, pH 8.2, 22.5% w/v PEG4000, and 200 mM magnesium chloride, at 10°C, 5 days. NAD-bound form crystals are obtained by soaking the apo-form crystal with a 001 ml crystallization reservoir containing 2 mM NAD+ molecule for about 30 min immediately prior X-ray diffraction, X-ray diffraction structure determination and analysis at 1.80-2.36 A resolution, molecular replacement and modelling, overview