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Literature summary extracted from

  • Takahashi-Iniguez, T.; Aburto-Rodriguez, N.; Vilchis-Gonzalez, A.; Flores, M.
    Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase (2016), J. Zhejiang Univ. Sci. B, 17, 247-261.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.37 L-malate at over 00.18 mM Pseudomonas stutzeri
1.1.1.37 NaCl activates at 3 M Haloarcula marismortui

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.37 gene mdh Haloarcula marismortui
1.1.1.37 gene mdh Bacillus subtilis
1.1.1.37 gene mdh Methanothermobacter thermautotrophicus
1.1.1.37 gene mdh Pseudomonas stutzeri
1.1.1.37 gene mdh Nitrosomonas europaea
1.1.1.37 gene mdh Corynebacterium glutamicum
1.1.1.37 gene mdh Streptomyces coelicolor
1.1.1.37 gene mdh Helicobacter pylori
1.1.1.37 gene mdh Kitasatospora aureofaciens
1.1.1.37 gene mdh Methanocaldococcus jannaschii
1.1.1.37 gene mdh Archaeoglobus fulgidus
1.1.1.37 gene mdh uncultured bacterium
1.1.1.37 gene mdh Glaesserella parasuis
1.1.1.37 gene mdh Aeropyrum pernix
1.1.1.82 gene mdh Bacillus subtilis
1.1.1.82 gene mdh Methanothermobacter thermautotrophicus
1.1.1.82 gene mdh Pseudomonas putida
1.1.1.82 gene mdh Methanocaldococcus jannaschii
1.1.1.82 gene mdh Aeropyrum pernix

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.37 crystal structure determination and analysis Escherichia coli
1.1.1.82 crystal structure determination and analysis Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.37 (S)-malate at 1 mM Methanothermobacter thermautotrophicus
1.1.1.37 2-oxoglutarate
-
 Pseudomonas stutzeri
1.1.1.37 ADP
-
 Pseudomonas stutzeri
1.1.1.37 Ag+
-
 Pseudomonas stutzeri
1.1.1.37 Citric acid
-
 Pseudomonas stutzeri
1.1.1.37 Cu2+
-
 Pseudomonas stutzeri
1.1.1.37 Fe2+
-
 Streptomyces coelicolor
1.1.1.37 L-malate MDH activity is strongly inhibited by excess of L-malate Streptomyces coelicolor
1.1.1.37 NAD+ MDH activity is inhibited by 0.5 mM NADH Methanothermobacter thermautotrophicus
1.1.1.37 NAD+
-
 Pseudomonas stutzeri
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Aeropyrum pernix
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH, over 2 mM Archaeoglobus fulgidus
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Bacillus subtilis
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM Corynebacterium glutamicum
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Escherichia coli
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Glaesserella parasuis
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Haloarcula marismortui
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Helicobacter pylori
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Kitasatospora aureofaciens
1.1.1.37 NADH MDH activity is inhibited by over 200 mM NADH Methanothermobacter thermautotrophicus
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH Nitrosomonas europaea
1.1.1.37 NADH MDH activity is strongly inhibited by excess of oxaloacetate and NADH uncultured bacterium
1.1.1.37 oxalic acid inhibits L-malate oxidation reaction Pseudomonas stutzeri
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Aeropyrum pernix
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH, overv 2 mM Archaeoglobus fulgidus
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Bacillus subtilis
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM Corynebacterium glutamicum
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Escherichia coli
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Glaesserella parasuis
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Haloarcula marismortui
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Helicobacter pylori
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Kitasatospora aureofaciens
1.1.1.37 oxaloacetate
-
 Methanothermobacter thermautotrophicus
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate and NADH Nitrosomonas europaea
1.1.1.37 oxaloacetate MDH activity is inhibited at 0.33 mM Pseudomonas stutzeri
1.1.1.37 oxaloacetate MDH activity is strongly inhibited by excess of oxaloacetate Streptomyces coelicolor
1.1.1.37 oxaloacetate MDH activity is inhibited by over 250 mM oxaloacetate uncultured bacterium
1.1.1.37 Zn2+
-
 Streptomyces coelicolor
1.1.1.82 NADPH MDH activity is inhibited by over 200 mM NADPH Methanothermobacter thermautotrophicus
1.1.1.82 oxaloacetate
-
 Methanothermobacter thermautotrophicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Haloarcula marismortui
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Escherichia coli
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Methanothermobacter thermautotrophicus
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas stutzeri
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Nitrosomonas europaea
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Corynebacterium glutamicum
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Streptomyces coelicolor
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Helicobacter pylori
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Kitasatospora aureofaciens
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Archaeoglobus fulgidus
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics uncultured bacterium
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Glaesserella parasuis
1.1.1.37 additional information
-
 additional information Michaelis-Menten kinetics Aeropyrum pernix
1.1.1.37 0.0001
-
 oxaloacetate pH and temperature not specified in the publication with NAD+ Kitasatospora aureofaciens
1.1.1.37 0.00012
-
 (S)-malate pH and temperature not specified in the publication Escherichia coli
1.1.1.37 0.00087
-
 NAD+ pH and temperature not specified in the publication Escherichia coli
1.1.1.37 0.014
-
 NADH pH and temperature not specified in the publication Bacillus subtilis
1.1.1.37 0.0165
-
 NADH pH and temperature not specified in the publication Glaesserella parasuis
1.1.1.37 0.0189
-
 oxaloacetate pH and temperature not specified in the publication Streptomyces coelicolor
1.1.1.37 0.02
-
 oxaloacetate pH and temperature not specified in the publication Nitrosomonas europaea
1.1.1.37 0.022
-
 NADH pH and temperature not specified in the publication Nitrosomonas europaea
1.1.1.37 0.022
-
 oxaloacetate pH and temperature not specified in the publication Bacillus subtilis
1.1.1.37 0.024
-
 NAD+ pH and temperature not specified in the publication Nitrosomonas europaea
1.1.1.37 0.024
-
 NADH pH and temperature not specified in the publication Archaeoglobus fulgidus
1.1.1.37 0.03
-
 NADH pH and temperature not specified in the publication uncultured bacterium
1.1.1.37 0.03
-
 oxaloacetate pH and temperature not specified in the publication Methanothermobacter thermautotrophicus
1.1.1.37 0.032
-
 oxaloacetate pH and temperature not specified in the publication Pseudomonas stutzeri
1.1.1.37 0.036
-
 NADH pH and temperature not specified in the publication Pseudomonas stutzeri
1.1.1.37 0.043
-
 oxaloacetate pH and temperature not specified in the publication Archaeoglobus fulgidus
1.1.1.37 0.05
-
 oxaloacetate pH and temperature not specified in the publication uncultured bacterium
1.1.1.37 0.063
-
 (S)-malate at 0.08-0.18 mM, pH and temperature not specified in the publication Pseudomonas stutzeri
1.1.1.37 0.065
-
 NADH pH and temperature not specified in the publication Helicobacter pylori
1.1.1.37 0.072
-
 oxaloacetate pH and temperature not specified in the publication Glaesserella parasuis
1.1.1.37 0.083
-
 NADH pH and temperature not specified in the publication Streptomyces coelicolor
1.1.1.37 0.085
-
 NADH pH and temperature not specified in the publication Kitasatospora aureofaciens
1.1.1.37 0.09
-
 NAD+ pH and temperature not specified in the publication Methanothermobacter thermautotrophicus
1.1.1.37 0.09
-
 NADH pH and temperature not specified in the publication Methanothermobacter thermautotrophicus
1.1.1.37 0.1
-
 NAD+ pH and temperature not specified in the publication Bacillus subtilis
1.1.1.37 0.117
-
 NAD+ pH and temperature not specified in the publication Glaesserella parasuis
1.1.1.37 0.12
-
 (S)-malate pH and temperature not specified in the publication Aeropyrum pernix
1.1.1.37 0.128
-
 oxaloacetate pH and temperature not specified in the publication Helicobacter pylori
1.1.1.37 0.15
-
 NAD+ pH and temperature not specified in the publication Streptomyces coelicolor
1.1.1.37 0.161
-
 NAD+ pH and temperature not specified in the publication Helicobacter pylori
1.1.1.37 0.177
-
 (S)-malate pH and temperature not specified in the publication Helicobacter pylori
1.1.1.37 0.26
-
 (S)-malate pH and temperature not specified in the publication Bacillus subtilis
1.1.1.37 0.27
-
 NAD+ pH and temperature not specified in the publication Kitasatospora aureofaciens
1.1.1.37 0.34
-
 NAD+ pH and temperature not specified in the publication Pseudomonas stutzeri
1.1.1.37 0.4
-
 (S)-malate pH and temperature not specified in the publication Methanothermobacter thermautotrophicus
1.1.1.37 0.49
-
 (S)-malate pH and temperature not specified in the publication Streptomyces coelicolor
1.1.1.37 0.55
-
 (S)-malate pH and temperature not specified in the publication Glaesserella parasuis
1.1.1.37 0.67
-
 (S)-malate at 0.18-10.0 mM, pH and temperature not specified in the publication Pseudomonas stutzeri
1.1.1.37 0.87
-
 NAD+ pH and temperature not specified in the publication Aeropyrum pernix
1.1.1.37 1.1
-
 NAD+ pH and temperature not specified in the publication uncultured bacterium
1.1.1.37 4
-
 (S)-malate pH and temperature not specified in the publication uncultured bacterium
1.1.1.37 5
-
 (S)-malate pH and temperature not specified in the publication Nitrosomonas europaea
1.1.1.37 9
-
 (S)-malate pH and temperature not specified in the publication Kitasatospora aureofaciens
1.1.1.82 additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
1.1.1.82 additional information
-
 additional information Michaelis-Menten kinetics Thermus thermophilus
1.1.1.82 additional information
-
 additional information Michaelis-Menten kinetics Methanothermobacter thermautotrophicus
1.1.1.82 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas putida
1.1.1.82 additional information
-
 additional information Michaelis-Menten kinetics Aeropyrum pernix
1.1.1.82 0.000019
-
 NADP+ pH and temperature not specified in the publication Thermus thermophilus
1.1.1.82 0.000019
-
 NADP+ pH and temperature not specified in the publication Aeropyrum pernix
1.1.1.82 0.00012
-
 (S)-malate pH and temperature not specified in the publication Thermus thermophilus
1.1.1.82 0.00012
-
 (S)-malate pH and temperature not specified in the publication Aeropyrum pernix
1.1.1.82 0.019
-
 NADP+ pH and temperature not specified in the publication Aeropyrum pernix
1.1.1.82 0.02
-
 NADPH pH and temperature not specified in the publication Methanothermobacter thermautotrophicus
1.1.1.82 0.023
-
 NADP+ pH and temperature not specified in the publication Pseudomonas putida
1.1.1.82 0.03
-
 oxaloacetate pH and temperature not specified in the publication Methanothermobacter thermautotrophicus
1.1.1.82 0.13
-
 NADP+ pH and temperature not specified in the publication Bacillus subtilis
1.1.1.82 0.26
-
 (S)-malate pH and temperature not specified in the publication Bacillus subtilis
1.1.1.82 0.4
-
 (S)-malate pH and temperature not specified in the publication Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.37 (S)-malate + NAD+ Haloarcula marismortui
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Bacillus subtilis
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Escherichia coli
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Methanothermobacter thermautotrophicus
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Pseudomonas stutzeri
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Nitrosomonas europaea
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Corynebacterium glutamicum
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Streptomyces coelicolor
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Helicobacter pylori
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Kitasatospora aureofaciens
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Methanocaldococcus jannaschii
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Archaeoglobus fulgidus
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ uncultured bacterium
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Glaesserella parasuis
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Aeropyrum pernix
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ uncultured bacterium MPOB
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Bacillus subtilis B1
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Haloarcula marismortui
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Bacillus subtilis
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Escherichia coli
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Methanothermobacter thermautotrophicus
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Pseudomonas stutzeri
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Nitrosomonas europaea
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Corynebacterium glutamicum
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Streptomyces coelicolor
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Helicobacter pylori
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Kitasatospora aureofaciens
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Methanocaldococcus jannaschii
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Archaeoglobus fulgidus
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ uncultured bacterium
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Glaesserella parasuis
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Aeropyrum pernix
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ uncultured bacterium MPOB
-
 (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+ Bacillus subtilis B1
-
 (S)-malate + NAD+
-
 r
1.1.1.82 (S)-malate + NADP+ Bacillus subtilis
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Thermus thermophilus
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Methanothermobacter thermautotrophicus
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Pseudomonas putida
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Methanocaldococcus jannaschii
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Aeropyrum pernix
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Thermus thermophilus AT-62
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+ Bacillus subtilis B1
-
 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Bacillus subtilis
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Thermus thermophilus
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Methanothermobacter thermautotrophicus
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Pseudomonas putida
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Methanocaldococcus jannaschii
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Aeropyrum pernix
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Thermus thermophilus AT-62
-
 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+ Bacillus subtilis B1
-
 (S)-malate + NADP+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Aeropyrum pernix
-
-
-
1.1.1.37 Archaeoglobus fulgidus
-
-
-
1.1.1.37 Bacillus subtilis
-
-
-
1.1.1.37 Bacillus subtilis B1
-
-
-
1.1.1.37 Corynebacterium glutamicum
-
-
-
1.1.1.37 Escherichia coli
-
-
-
1.1.1.37 Glaesserella parasuis
-
-
-
1.1.1.37 Haloarcula marismortui
-
-
-
1.1.1.37 Helicobacter pylori
-
-
-
1.1.1.37 Kitasatospora aureofaciens
-
-
-
1.1.1.37 Methanocaldococcus jannaschii
-
-
-
1.1.1.37 Methanothermobacter thermautotrophicus
-
-
-
1.1.1.37 Nitrosomonas europaea
-
-
-
1.1.1.37 Pseudomonas stutzeri
-
-
-
1.1.1.37 Streptomyces coelicolor
-
-
-
1.1.1.37 uncultured bacterium
-
 a syntropic propionate-oxidizing strain
-
1.1.1.37 uncultured bacterium MPOB
-
 a syntropic propionate-oxidizing strain
-
1.1.1.82 Aeropyrum pernix
-
-
-
1.1.1.82 Bacillus subtilis
-
-
-
1.1.1.82 Bacillus subtilis B1
-
-
-
1.1.1.82 Methanocaldococcus jannaschii
-
-
-
1.1.1.82 Methanothermobacter thermautotrophicus
-
-
-
1.1.1.82 Pseudomonas putida
-
-
-
1.1.1.82 Thermus thermophilus
-
-
-
1.1.1.82 Thermus thermophilus AT-62
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.37 additional information increased enzyme content in cells grown on acid media Escherichia coli
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.37 (S)-malate + NAD+
-
 Haloarcula marismortui oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Bacillus subtilis oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Escherichia coli oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Methanothermobacter thermautotrophicus oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Pseudomonas stutzeri oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Nitrosomonas europaea oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Corynebacterium glutamicum oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Streptomyces coelicolor oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Helicobacter pylori oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Kitasatospora aureofaciens oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Methanocaldococcus jannaschii oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Archaeoglobus fulgidus oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 uncultured bacterium oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Glaesserella parasuis oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Aeropyrum pernix oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 uncultured bacterium MPOB oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Bacillus subtilis B1 oxaloacetate + NADH + H+
-
 r
1.1.1.37 additional information the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii Methanocaldococcus jannaschii ?
-
 ?
1.1.1.37 oxaloacetate + NADH + H+
-
 Haloarcula marismortui (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Bacillus subtilis (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Escherichia coli (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Methanothermobacter thermautotrophicus (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Pseudomonas stutzeri (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Nitrosomonas europaea (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Corynebacterium glutamicum (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Streptomyces coelicolor (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Helicobacter pylori (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Kitasatospora aureofaciens (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Archaeoglobus fulgidus (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 uncultured bacterium (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Glaesserella parasuis (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Aeropyrum pernix (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 uncultured bacterium MPOB (S)-malate + NAD+
-
 r
1.1.1.37 oxaloacetate + NADH + H+
-
 Bacillus subtilis B1 (S)-malate + NAD+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Bacillus subtilis oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Thermus thermophilus oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Methanothermobacter thermautotrophicus oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Pseudomonas putida oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Methanocaldococcus jannaschii oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Aeropyrum pernix oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Thermus thermophilus AT-62 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 (S)-malate + NADP+
-
 Bacillus subtilis B1 oxaloacetate + NADPH + H+
-
 r
1.1.1.82 additional information the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii Methanocaldococcus jannaschii ?
-
 ?
1.1.1.82 additional information the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 Bacillus subtilis ?
-
 ?
1.1.1.82 additional information the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 Methanothermobacter thermautotrophicus ?
-
 ?
1.1.1.82 additional information the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 Pseudomonas putida ?
-
 ?
1.1.1.82 additional information the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 Aeropyrum pernix ?
-
 ?
1.1.1.82 additional information the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 Bacillus subtilis B1 ?
-
 ?
1.1.1.82 oxaloacetate + NADPH + H+
-
 Bacillus subtilis (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Thermus thermophilus (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Methanothermobacter thermautotrophicus (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Pseudomonas putida (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Aeropyrum pernix (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Thermus thermophilus AT-62 (S)-malate + NADP+
-
 r
1.1.1.82 oxaloacetate + NADPH + H+
-
 Bacillus subtilis B1 (S)-malate + NADP+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.37 More oligomeric states of MDHs, overview Haloarcula marismortui
1.1.1.37 More oligomeric states of MDHs, overview Bacillus subtilis
1.1.1.37 More oligomeric states of MDHs, overview Methanothermobacter thermautotrophicus
1.1.1.37 More oligomeric states of MDHs, overview Pseudomonas stutzeri
1.1.1.37 More oligomeric states of MDHs, overview Nitrosomonas europaea
1.1.1.37 More oligomeric states of MDHs, overview Corynebacterium glutamicum
1.1.1.37 More oligomeric states of MDHs, overview Streptomyces coelicolor
1.1.1.37 More oligomeric states of MDHs, overview Helicobacter pylori
1.1.1.37 More oligomeric states of MDHs, overview Kitasatospora aureofaciens
1.1.1.37 More oligomeric states of MDHs, overview Archaeoglobus fulgidus
1.1.1.37 More oligomeric states of MDHs, overview uncultured bacterium
1.1.1.37 More oligomeric states of MDHs, overview Glaesserella parasuis
1.1.1.37 More oligomeric states of MDHs, overview Aeropyrum pernix
1.1.1.82 monomer
-
 Thermus thermophilus
1.1.1.82 More oligomeric states of MDHs, overview Bacillus subtilis
1.1.1.82 More oligomeric states of MDHs, overview Methanothermobacter thermautotrophicus
1.1.1.82 More oligomeric states of MDHs, overview Pseudomonas putida
1.1.1.82 More oligomeric states of MDHs, overview Aeropyrum pernix

Synonyms

EC Number Synonyms Comment Organism
1.1.1.37 L-malate:NAD oxidoreductase
-
 Haloarcula marismortui
1.1.1.37 L-malate:NAD oxidoreductase
-
 Bacillus subtilis
1.1.1.37 L-malate:NAD oxidoreductase
-
 Escherichia coli
1.1.1.37 L-malate:NAD oxidoreductase
-
 Methanothermobacter thermautotrophicus
1.1.1.37 L-malate:NAD oxidoreductase
-
 Pseudomonas stutzeri
1.1.1.37 L-malate:NAD oxidoreductase
-
 Nitrosomonas europaea
1.1.1.37 L-malate:NAD oxidoreductase
-
 Corynebacterium glutamicum
1.1.1.37 L-malate:NAD oxidoreductase
-
 Streptomyces coelicolor
1.1.1.37 L-malate:NAD oxidoreductase
-
 Helicobacter pylori
1.1.1.37 L-malate:NAD oxidoreductase
-
 Kitasatospora aureofaciens
1.1.1.37 L-malate:NAD oxidoreductase
-
 Methanocaldococcus jannaschii
1.1.1.37 L-malate:NAD oxidoreductase
-
 Archaeoglobus fulgidus
1.1.1.37 L-malate:NAD oxidoreductase
-
 uncultured bacterium
1.1.1.37 L-malate:NAD oxidoreductase
-
 Glaesserella parasuis
1.1.1.37 L-malate:NAD oxidoreductase
-
 Aeropyrum pernix
1.1.1.37 MDH
-
 Haloarcula marismortui
1.1.1.37 MDH
-
 Bacillus subtilis
1.1.1.37 MDH
-
 Escherichia coli
1.1.1.37 MDH
-
 Methanothermobacter thermautotrophicus
1.1.1.37 MDH
-
 Pseudomonas stutzeri
1.1.1.37 MDH
-
 Nitrosomonas europaea
1.1.1.37 MDH
-
 Corynebacterium glutamicum
1.1.1.37 MDH
-
 Streptomyces coelicolor
1.1.1.37 MDH
-
 Helicobacter pylori
1.1.1.37 MDH
-
 Kitasatospora aureofaciens
1.1.1.37 MDH
-
 Methanocaldococcus jannaschii
1.1.1.37 MDH
-
 Archaeoglobus fulgidus
1.1.1.37 MDH
-
 uncultured bacterium
1.1.1.37 MDH
-
 Glaesserella parasuis
1.1.1.37 MDH
-
 Aeropyrum pernix
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Haloarcula marismortui
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Bacillus subtilis
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Escherichia coli
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Methanothermobacter thermautotrophicus
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Pseudomonas stutzeri
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Nitrosomonas europaea
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Corynebacterium glutamicum
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Streptomyces coelicolor
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Helicobacter pylori
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Kitasatospora aureofaciens
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Archaeoglobus fulgidus
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 uncultured bacterium
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Glaesserella parasuis
1.1.1.37 NAD+-dependent malate dehydrogenase
-
 Aeropyrum pernix
1.1.1.37 NADP+-dependent malate dehydrogenase
-
 Methanocaldococcus jannaschii
1.1.1.82 L-malate:NAD oxidoreductase
-
 Bacillus subtilis
1.1.1.82 L-malate:NAD oxidoreductase
-
 Aeropyrum pernix
1.1.1.82 MDH
-
 Bacillus subtilis
1.1.1.82 MDH
-
 Thermus thermophilus
1.1.1.82 MDH
-
 Methanothermobacter thermautotrophicus
1.1.1.82 MDH
-
 Pseudomonas putida
1.1.1.82 MDH
-
 Methanocaldococcus jannaschii
1.1.1.82 MDH
-
 Aeropyrum pernix
1.1.1.82 NADP+-dependent malate dehydrogenase
-
 Bacillus subtilis
1.1.1.82 NADP+-dependent malate dehydrogenase
-
 Thermus thermophilus
1.1.1.82 NADP+-dependent malate dehydrogenase
-
 Methanothermobacter thermautotrophicus
1.1.1.82 NADP+-dependent malate dehydrogenase
-
 Pseudomonas putida
1.1.1.82 NADP+-dependent malate dehydrogenase
-
 Methanocaldococcus jannaschii
1.1.1.82 NADP+-dependent malate dehydrogenase
-
 Aeropyrum pernix

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.37 NAD+
-
 Haloarcula marismortui
1.1.1.37 NAD+
-
 Bacillus subtilis
1.1.1.37 NAD+
-
 Methanothermobacter thermautotrophicus
1.1.1.37 NAD+
-
 Pseudomonas stutzeri
1.1.1.37 NAD+
-
 Nitrosomonas europaea
1.1.1.37 NAD+
-
 Corynebacterium glutamicum
1.1.1.37 NAD+
-
 Streptomyces coelicolor
1.1.1.37 NAD+
-
 Helicobacter pylori
1.1.1.37 NAD+
-
 Kitasatospora aureofaciens
1.1.1.37 NAD+
-
 Methanocaldococcus jannaschii
1.1.1.37 NAD+
-
 Archaeoglobus fulgidus
1.1.1.37 NAD+
-
 uncultured bacterium
1.1.1.37 NAD+
-
 Glaesserella parasuis
1.1.1.37 NAD+
-
 Aeropyrum pernix
1.1.1.37 NAD+ the ribose from NAD+ interacts with residues Gly10, Gly11, Ile12, Gly78, Val79, Asn119, Tyr33, Asp34, Ala77, Ile97, Leu101, Ser76, Ile117, Val146, and Met227 Escherichia coli
1.1.1.37 NADH
-
 Haloarcula marismortui
1.1.1.37 NADH
-
 Bacillus subtilis
1.1.1.37 NADH
-
 Escherichia coli
1.1.1.37 NADH
-
 Methanothermobacter thermautotrophicus
1.1.1.37 NADH
-
 Pseudomonas stutzeri
1.1.1.37 NADH
-
 Nitrosomonas europaea
1.1.1.37 NADH
-
 Corynebacterium glutamicum
1.1.1.37 NADH
-
 Streptomyces coelicolor
1.1.1.37 NADH
-
 Helicobacter pylori
1.1.1.37 NADH
-
 Kitasatospora aureofaciens
1.1.1.37 NADH
-
 Methanocaldococcus jannaschii
1.1.1.37 NADH
-
 Archaeoglobus fulgidus
1.1.1.37 NADH
-
 uncultured bacterium
1.1.1.37 NADH
-
 Glaesserella parasuis
1.1.1.37 NADH
-
 Aeropyrum pernix
1.1.1.82 NADP+
-
 Bacillus subtilis
1.1.1.82 NADP+
-
 Thermus thermophilus
1.1.1.82 NADP+
-
 Methanothermobacter thermautotrophicus
1.1.1.82 NADP+
-
 Pseudomonas putida
1.1.1.82 NADP+
-
 Aeropyrum pernix
1.1.1.82 NADP+ NADP+ binds to Ser9, Arg34, His36, Ser37, Ile121, Asn123, and Glu219 Methanocaldococcus jannaschii
1.1.1.82 NADPH
-
 Bacillus subtilis
1.1.1.82 NADPH
-
 Methanothermobacter thermautotrophicus
1.1.1.82 NADPH
-
 Pseudomonas putida
1.1.1.82 NADPH
-
 Methanocaldococcus jannaschii
1.1.1.82 NADPH
-
 Aeropyrum pernix
1.1.1.82 NADPH nicotinamide binds to the hydrophobic cleft of MDH from Thermus flavus composed of Leu40, Ile42, Ile107, Thr9, Gly10, Gly87, and Ala88 Thermus thermophilus

Expression

EC Number Organism Comment Expression
1.1.1.37 Escherichia coli the enzyme expression is downregulated by the aerobic respiration control protein (ArcA), particularly under anaerobic conditions down
1.1.1.37 Haloarcula marismortui transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Bacillus subtilis transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Methanothermobacter thermautotrophicus transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Pseudomonas stutzeri transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Nitrosomonas europaea transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Corynebacterium glutamicum transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Streptomyces coelicolor transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Helicobacter pylori transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Kitasatospora aureofaciens transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Methanocaldococcus jannaschii transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Archaeoglobus fulgidus transcriptional regulation of mdh gene, overview additional information
1.1.1.37 uncultured bacterium transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Glaesserella parasuis transcriptional regulation of mdh gene, overview additional information
1.1.1.37 Aeropyrum pernix transcriptional regulation of mdh gene, overview additional information
1.1.1.82 Bacillus subtilis transcriptional regulation of mdh gene, overview additional information
1.1.1.82 Methanothermobacter thermautotrophicus transcriptional regulation of mdh gene, overview additional information
1.1.1.82 Pseudomonas putida transcriptional regulation of mdh gene, overview additional information
1.1.1.82 Methanocaldococcus jannaschii transcriptional regulation of mdh gene, overview additional information
1.1.1.82 Aeropyrum pernix transcriptional regulation of mdh gene, overview additional information

General Information

EC Number General Information Comment Organism
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus. The other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Kitasatospora aureofaciens
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Haloarcula marismortui
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Bacillus subtilis
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Escherichia coli
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Methanothermobacter thermautotrophicus
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Pseudomonas stutzeri
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Nitrosomonas europaea
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Corynebacterium glutamicum
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Streptomyces coelicolor
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Helicobacter pylori
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Methanocaldococcus jannaschii
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Archaeoglobus fulgidus
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview uncultured bacterium
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Glaesserella parasuis
1.1.1.37 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Aeropyrum pernix
1.1.1.37 physiological function regulation of MDH activity, overview Haloarcula marismortui
1.1.1.37 physiological function regulation of MDH activity, overview Bacillus subtilis
1.1.1.37 physiological function regulation of MDH activity, overview Methanothermobacter thermautotrophicus
1.1.1.37 physiological function regulation of MDH activity, overview Pseudomonas stutzeri
1.1.1.37 physiological function regulation of MDH activity, overview Nitrosomonas europaea
1.1.1.37 physiological function regulation of MDH activity, overview Corynebacterium glutamicum
1.1.1.37 physiological function regulation of MDH activity, overview Streptomyces coelicolor
1.1.1.37 physiological function regulation of MDH activity, overview Helicobacter pylori
1.1.1.37 physiological function regulation of MDH activity, overview Kitasatospora aureofaciens
1.1.1.37 physiological function regulation of MDH activity, overview Methanocaldococcus jannaschii
1.1.1.37 physiological function regulation of MDH activity, overview Archaeoglobus fulgidus
1.1.1.37 physiological function regulation of MDH activity, overview uncultured bacterium
1.1.1.37 physiological function regulation of MDH activity, overview Glaesserella parasuis
1.1.1.37 physiological function regulation of MDH activity, overview Aeropyrum pernix
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus, the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Thermus thermophilus
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH) Aeropyrum pernix
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Bacillus subtilis
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Methanothermobacter thermautotrophicus
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Pseudomonas putida
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Methanocaldococcus jannaschii
1.1.1.82 evolution MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview Aeropyrum pernix
1.1.1.82 physiological function regulation of MDH activity, overview Bacillus subtilis
1.1.1.82 physiological function regulation of MDH activity, overview Methanothermobacter thermautotrophicus
1.1.1.82 physiological function regulation of MDH activity, overview Pseudomonas putida
1.1.1.82 physiological function regulation of MDH activity, overview Methanocaldococcus jannaschii
1.1.1.82 physiological function regulation of MDH activity, overview Aeropyrum pernix