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Literature summary extracted from

  • Yin, Y.; Kirsch, J.F.
    Identification of functional paralog shift mutations: conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase (2007), Proc. Natl. Acad. Sci. USA, 104, 17353-17357.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.37 gene mdh, expression of wild-type and mutant enzymes in strains DH10B and W945T1-2 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.27 additional information the malate dehydrogenase, EC 1.1.1.37, mutant I12V/R81Q/M85E/G210A/V214I shows a substrate specificity that is switched from malate dehydrogenase to that of lactate dehydrogenase, overview Escherichia coli
1.1.1.27 additional information the malate dehydrogenase, EC 1.1.1.37, mutant I12V/R81Q/M85E/G210A/V214I shows a substrate specificity that is switched from malate dehydrogenase to that of lactate dehydrogenase, overview Geobacillus stearothermophilus
1.1.1.37 F144I site-directed mutagenesis, inactive mutant Escherichia coli
1.1.1.37 G210A site-directed mutagenesis, the mutant shows 30% reduced activity compared to the wild-type enzyme Escherichia coli
1.1.1.37 G210A/V214I site-directed mutagenesis, the double mutant shows a 2.2fold increase in lacatate dehydrogenase activity compared to the wild-type enzyme Escherichia coli
1.1.1.37 I12V/R81Q/M85E/G210A/V214I construction of a pentamutant by site-directed mutagenesis, whose substrate specificity is switched from malate dehydrogenase to that of lactate dehydrogenase, EC 1.1.1.27, the mutant shows highly reduced activity compared to the wild-type enzyme, overview Escherichia coli
1.1.1.37 N122D site-directed mutagenesis, inactive mutant Escherichia coli
1.1.1.37 R81Q site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Escherichia coli
1.1.1.37 V214I site-directed mutagenesis, the mutant's activity is not affected Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 0.06
-
 pyruvate pH 6.0, 25°C, recombinant wild-type enzyme Geobacillus stearothermophilus
1.1.1.27 13.3
-
 pyruvate pH 7.5, 25°C, recombinant mutant I12V/R81Q/M85E/G210A/V214I Escherichia coli
1.1.1.37 0.04
-
 oxaloacetate pH 7.5, 30°C,recombinant wild-type enzyme Escherichia coli
1.1.1.37 3
-
 oxaloacetate pH 7.5, 30°C, recombinant mutant R81Q Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+ Geobacillus stearothermophilus
-
 pyruvate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Escherichia coli
-
 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ Escherichia coli MG1655
-
 oxaloacetate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Escherichia coli
-
-
-
1.1.1.27 Geobacillus stearothermophilus P00344 gene ldh
-
1.1.1.37 Escherichia coli P61889 gene mdh
-
1.1.1.37 Escherichia coli MG1655 P61889 gene mdh
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.27 additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+
-
 Geobacillus stearothermophilus pyruvate + NADH + H+
-
 r
1.1.1.27 (S)-lactate + NAD+ mutant I12V/R81Q/M85E/G210A/V214I, residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity Escherichia coli pyruvate + NADH + H+
-
 r
1.1.1.27 (S)-lactate + NAD+ residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity Geobacillus stearothermophilus pyruvate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Escherichia coli oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity Escherichia coli oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+
-
 Escherichia coli MG1655 oxaloacetate + NADH + H+
-
 r
1.1.1.37 (S)-malate + NAD+ residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity Escherichia coli MG1655 oxaloacetate + NADH + H+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.27 lactate dehydrogenase
-
 Escherichia coli
1.1.1.27 lactate dehydrogenase
-
 Geobacillus stearothermophilus
1.1.1.27 LDH
-
 Escherichia coli
1.1.1.27 LDH
-
 Geobacillus stearothermophilus
1.1.1.37 malate dehydrogenase
-
 Escherichia coli
1.1.1.37 MDH
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.27 25
-
 assay at Geobacillus stearothermophilus
1.1.1.27 30
-
 assay at Escherichia coli
1.1.1.37 30
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.27 46.5
-
 pyruvate pH 7.5, 25°C, recombinant mutant I12V/R81Q/M85E/G210A/V214I Escherichia coli
1.1.1.27 250
-
 pyruvate pH 6.0, 25°C, recombinant wild-type enzyme Geobacillus stearothermophilus
1.1.1.37 0.77
-
 oxaloacetate pH 7.5, 30°C, recombinant mutant R81Q Escherichia coli
1.1.1.37 931
-
 oxaloacetate pH 7.5, 30°C, recombinant wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.27 6
-
 assay at Geobacillus stearothermophilus
1.1.1.27 7.5
-
 assay at Escherichia coli
1.1.1.37 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+
-
 Escherichia coli
1.1.1.27 NAD+
-
 Geobacillus stearothermophilus
1.1.1.27 NADH
-
 Escherichia coli
1.1.1.27 NADH
-
 Geobacillus stearothermophilus