Cloned (Comment) | Organism |
---|---|
gene mdh | Bacillus subtilis |
gene mdh | Methanothermobacter thermautotrophicus |
gene mdh | Pseudomonas putida |
gene mdh | Methanocaldococcus jannaschii |
gene mdh | Aeropyrum pernix |
Crystallization (Comment) | Organism |
---|---|
crystal structure determination and analysis | Thermus thermophilus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NADPH | MDH activity is inhibited by over 200 mM NADPH | Methanothermobacter thermautotrophicus | |
oxaloacetate | - |
Methanothermobacter thermautotrophicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Bacillus subtilis | |
additional information | - |
additional information | Michaelis-Menten kinetics | Thermus thermophilus | |
additional information | - |
additional information | Michaelis-Menten kinetics | Methanothermobacter thermautotrophicus | |
additional information | - |
additional information | Michaelis-Menten kinetics | Pseudomonas putida | |
additional information | - |
additional information | Michaelis-Menten kinetics | Aeropyrum pernix | |
0.000019 | - |
NADP+ | pH and temperature not specified in the publication | Thermus thermophilus | |
0.000019 | - |
NADP+ | pH and temperature not specified in the publication | Aeropyrum pernix | |
0.00012 | - |
(S)-malate | pH and temperature not specified in the publication | Thermus thermophilus | |
0.00012 | - |
(S)-malate | pH and temperature not specified in the publication | Aeropyrum pernix | |
0.019 | - |
NADP+ | pH and temperature not specified in the publication | Aeropyrum pernix | |
0.02 | - |
NADPH | pH and temperature not specified in the publication | Methanothermobacter thermautotrophicus | |
0.023 | - |
NADP+ | pH and temperature not specified in the publication | Pseudomonas putida | |
0.03 | - |
oxaloacetate | pH and temperature not specified in the publication | Methanothermobacter thermautotrophicus | |
0.13 | - |
NADP+ | pH and temperature not specified in the publication | Bacillus subtilis | |
0.26 | - |
(S)-malate | pH and temperature not specified in the publication | Bacillus subtilis | |
0.4 | - |
(S)-malate | pH and temperature not specified in the publication | Pseudomonas putida |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NADP+ | Bacillus subtilis | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Thermus thermophilus | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Methanothermobacter thermautotrophicus | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Pseudomonas putida | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Methanocaldococcus jannaschii | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Aeropyrum pernix | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Thermus thermophilus AT-62 | - |
oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | Bacillus subtilis B1 | - |
oxaloacetate + NADPH + H+ | - |
r | |
oxaloacetate + NADPH + H+ | Bacillus subtilis | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Thermus thermophilus | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Methanothermobacter thermautotrophicus | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Pseudomonas putida | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Methanocaldococcus jannaschii | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Aeropyrum pernix | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Thermus thermophilus AT-62 | - |
(S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | Bacillus subtilis B1 | - |
(S)-malate + NADP+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | - |
- |
- |
Bacillus subtilis | - |
- |
- |
Bacillus subtilis B1 | - |
- |
- |
Methanocaldococcus jannaschii | - |
- |
- |
Methanothermobacter thermautotrophicus | - |
- |
- |
Pseudomonas putida | - |
- |
- |
Thermus thermophilus | - |
- |
- |
Thermus thermophilus AT-62 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NADP+ | - |
Bacillus subtilis | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Thermus thermophilus | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Methanothermobacter thermautotrophicus | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Pseudomonas putida | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Methanocaldococcus jannaschii | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Aeropyrum pernix | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Thermus thermophilus AT-62 | oxaloacetate + NADPH + H+ | - |
r | |
(S)-malate + NADP+ | - |
Bacillus subtilis B1 | oxaloacetate + NADPH + H+ | - |
r | |
additional information | the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii | Methanocaldococcus jannaschii | ? | - |
? | |
additional information | the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 | Bacillus subtilis | ? | - |
? | |
additional information | the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 | Methanothermobacter thermautotrophicus | ? | - |
? | |
additional information | the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 | Pseudomonas putida | ? | - |
? | |
additional information | the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 | Aeropyrum pernix | ? | - |
? | |
additional information | the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33 | Bacillus subtilis B1 | ? | - |
? | |
oxaloacetate + NADPH + H+ | - |
Bacillus subtilis | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Thermus thermophilus | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Methanothermobacter thermautotrophicus | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Pseudomonas putida | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Methanocaldococcus jannaschii | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Aeropyrum pernix | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Thermus thermophilus AT-62 | (S)-malate + NADP+ | - |
r | |
oxaloacetate + NADPH + H+ | - |
Bacillus subtilis B1 | (S)-malate + NADP+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Thermus thermophilus |
More | oligomeric states of MDHs, overview | Bacillus subtilis |
More | oligomeric states of MDHs, overview | Methanothermobacter thermautotrophicus |
More | oligomeric states of MDHs, overview | Pseudomonas putida |
More | oligomeric states of MDHs, overview | Aeropyrum pernix |
Synonyms | Comment | Organism |
---|---|---|
L-malate:NAD oxidoreductase | - |
Bacillus subtilis |
L-malate:NAD oxidoreductase | - |
Aeropyrum pernix |
MDH | - |
Bacillus subtilis |
MDH | - |
Thermus thermophilus |
MDH | - |
Methanothermobacter thermautotrophicus |
MDH | - |
Pseudomonas putida |
MDH | - |
Methanocaldococcus jannaschii |
MDH | - |
Aeropyrum pernix |
NADP+-dependent malate dehydrogenase | - |
Bacillus subtilis |
NADP+-dependent malate dehydrogenase | - |
Thermus thermophilus |
NADP+-dependent malate dehydrogenase | - |
Methanothermobacter thermautotrophicus |
NADP+-dependent malate dehydrogenase | - |
Pseudomonas putida |
NADP+-dependent malate dehydrogenase | - |
Methanocaldococcus jannaschii |
NADP+-dependent malate dehydrogenase | - |
Aeropyrum pernix |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Bacillus subtilis | |
NADP+ | - |
Thermus thermophilus | |
NADP+ | - |
Methanothermobacter thermautotrophicus | |
NADP+ | - |
Pseudomonas putida | |
NADP+ | - |
Aeropyrum pernix | |
NADP+ | NADP+ binds to Ser9, Arg34, His36, Ser37, Ile121, Asn123, and Glu219 | Methanocaldococcus jannaschii | |
NADPH | - |
Bacillus subtilis | |
NADPH | - |
Methanothermobacter thermautotrophicus | |
NADPH | - |
Pseudomonas putida | |
NADPH | - |
Methanocaldococcus jannaschii | |
NADPH | - |
Aeropyrum pernix | |
NADPH | nicotinamide binds to the hydrophobic cleft of MDH from Thermus flavus composed of Leu40, Ile42, Ile107, Thr9, Gly10, Gly87, and Ala88 | Thermus thermophilus |
Organism | Comment | Expression |
---|---|---|
Bacillus subtilis | transcriptional regulation of mdh gene, overview | additional information |
Methanothermobacter thermautotrophicus | transcriptional regulation of mdh gene, overview | additional information |
Pseudomonas putida | transcriptional regulation of mdh gene, overview | additional information |
Methanocaldococcus jannaschii | transcriptional regulation of mdh gene, overview | additional information |
Aeropyrum pernix | transcriptional regulation of mdh gene, overview | additional 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 | Thermus thermophilus |
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 |
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 | 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 putida |
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 | Aeropyrum pernix |
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 putida |
physiological function | regulation of MDH activity, overview | Methanocaldococcus jannaschii |
physiological function | regulation of MDH activity, overview | Aeropyrum pernix |