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Literature summary for 1.1.1.37 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

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

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determination and analysis Escherichia coli

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
Haloarcula marismortui oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Bacillus subtilis oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Escherichia coli oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Methanothermobacter thermautotrophicus oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Pseudomonas stutzeri oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Nitrosomonas europaea oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Corynebacterium glutamicum oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Streptomyces coelicolor oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Helicobacter pylori oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Kitasatospora aureofaciens oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Methanocaldococcus jannaschii oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Archaeoglobus fulgidus oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
uncultured bacterium oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Glaesserella parasuis oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Aeropyrum pernix oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
uncultured bacterium MPOB oxaloacetate + NADH + H+
-
r
(S)-malate + NAD+
-
Bacillus subtilis B1 oxaloacetate + NADH + H+
-
r
additional information the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii Methanocaldococcus jannaschii ?
-
?
oxaloacetate + NADH + H+
-
Haloarcula marismortui (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Bacillus subtilis (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Escherichia coli (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Methanothermobacter thermautotrophicus (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Pseudomonas stutzeri (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Nitrosomonas europaea (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Corynebacterium glutamicum (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Streptomyces coelicolor (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Helicobacter pylori (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Kitasatospora aureofaciens (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Methanocaldococcus jannaschii (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Archaeoglobus fulgidus (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
uncultured bacterium (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Glaesserella parasuis (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Aeropyrum pernix (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
uncultured bacterium MPOB (S)-malate + NAD+
-
r
oxaloacetate + NADH + H+
-
Bacillus subtilis B1 (S)-malate + NAD+
-
r

Subunits

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Haloarcula marismortui
NAD+
-
Bacillus subtilis
NAD+
-
Methanothermobacter thermautotrophicus
NAD+
-
Pseudomonas stutzeri
NAD+
-
Nitrosomonas europaea
NAD+
-
Corynebacterium glutamicum
NAD+
-
Streptomyces coelicolor
NAD+
-
Helicobacter pylori
NAD+
-
Kitasatospora aureofaciens
NAD+
-
Methanocaldococcus jannaschii
NAD+
-
Archaeoglobus fulgidus
NAD+
-
uncultured bacterium
NAD+
-
Glaesserella parasuis
NAD+
-
Aeropyrum pernix
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
NADH
-
Haloarcula marismortui
NADH
-
Bacillus subtilis
NADH
-
Escherichia coli
NADH
-
Methanothermobacter thermautotrophicus
NADH
-
Pseudomonas stutzeri
NADH
-
Nitrosomonas europaea
NADH
-
Corynebacterium glutamicum
NADH
-
Streptomyces coelicolor
NADH
-
Helicobacter pylori
NADH
-
Kitasatospora aureofaciens
NADH
-
Methanocaldococcus jannaschii
NADH
-
Archaeoglobus fulgidus
NADH
-
uncultured bacterium
NADH
-
Glaesserella parasuis
NADH
-
Aeropyrum pernix

Expression

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

General Information

General Information Comment Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
physiological function regulation of MDH activity, overview Haloarcula marismortui
physiological function regulation of MDH activity, overview Bacillus subtilis
physiological function regulation of MDH activity, overview Methanothermobacter thermautotrophicus
physiological function regulation of MDH activity, overview Pseudomonas stutzeri
physiological function regulation of MDH activity, overview Nitrosomonas europaea
physiological function regulation of MDH activity, overview Corynebacterium glutamicum
physiological function regulation of MDH activity, overview Streptomyces coelicolor
physiological function regulation of MDH activity, overview Helicobacter pylori
physiological function regulation of MDH activity, overview Kitasatospora aureofaciens
physiological function regulation of MDH activity, overview Methanocaldococcus jannaschii
physiological function regulation of MDH activity, overview Archaeoglobus fulgidus
physiological function regulation of MDH activity, overview uncultured bacterium
physiological function regulation of MDH activity, overview Glaesserella parasuis
physiological function regulation of MDH activity, overview Aeropyrum pernix