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Literature summary for 1.1.1.82 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

Cloned(Commentary)

Cloned (Comment) Organism
gene mdh Bacillus subtilis
gene mdh Methanothermobacter thermautotrophicus
gene mdh Pseudomonas putida
gene mdh Methanocaldococcus jannaschii
gene mdh Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determination and analysis Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
NADPH MDH activity is inhibited by over 200 mM NADPH Methanothermobacter thermautotrophicus
oxaloacetate
-
Methanothermobacter thermautotrophicus

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-
Bacillus subtilis
-
-
-
Bacillus subtilis B1
-
-
-
Methanocaldococcus jannaschii
-
-
-
Methanothermobacter thermautotrophicus
-
-
-
Pseudomonas putida
-
-
-
Thermus thermophilus
-
-
-
Thermus thermophilus AT-62
-
-
-

Substrates and Products (Substrate)

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

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

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

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

Expression

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

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