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Literature summary extracted from

  • Song, P.; Li, S.; Wu, Y.; Lv, C.; Wang, P.; Zhu, G.
    Point mutation (R153H or R153C) in Escherichia coli isocitrate dehydrogenase Biochemical characterization and functional implication (2017), J. Basic Microbiol., 57, 41-49 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.42 expressed in Escherichia coli Rosetta (DE3) cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.42 R153C the mutation dramatically reduces the catalytic efficiency of the enzyme for isocitrate oxidation, which drops to 1.5% of the wild type enzyme. The mutant acquires a neomorphic ability of producing 2-hydroxyglutarate from 2-oxoglutarate Escherichia coli
1.1.1.42 R153H the mutation dramatically reduces the catalytic efficiency of the enzyme for isocitrate oxidation, which drops to 0.6% of the wild type enzyme. The mutant acquires a neomorphic ability of producing 2-hydroxyglutarate from 2-oxoglutarate Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.42 0.00071
-
 NADPH mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.00072
-
 NADPH mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.011
-
 NADP+ mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.0121
-
 NADP+ wild type enzyme, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.0176
-
 NADP+ mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.0217
-
 isocitrate mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.0242
-
 isocitrate wild type enzyme, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.0318
-
 isocitrate mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 2.2
-
 2-oxoglutarate mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 3.3
-
 2-oxoglutarate mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.42 cytosol
-
 Escherichia coli 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.42 Mn2+ 2 mM used in assay conditions Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.42 isocitrate + NADP+ Escherichia coli
-
 2-oxoglutarate + CO2 + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.42 Escherichia coli P08200
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.42 TALON metal affinity resin column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.42 2-oxoglutarate + NADPH + H+ the reaction is catalyzed by mutant enzymes R153H and R153C Escherichia coli 2-hydroxyglutarate + NADP+
-
 ?
1.1.1.42 isocitrate + NADP+
-
 Escherichia coli 2-oxoglutarate + CO2 + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.42 ? x * 45000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.1.1.42 IDH1
-
 Escherichia coli
1.1.1.42 NADP+-IDH
-
 Escherichia coli
1.1.1.42 NADP+-isocitrate dehydrogenase
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.42 0.18
-
 isocitrate mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.3
-
 isocitrate mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 1
-
 2-oxoglutarate mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 1
-
 2-oxoglutarate mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 51.8
-
 isocitrate wild type enzyme, at pH 7.5 and 25°C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.42 NADP+
-
 Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.42 0.3
-
 2-oxoglutarate mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 0.45
-
 2-oxoglutarate mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 8
-
 isocitrate mutant enzyme R153H, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 9
-
 isocitrate mutant enzyme R153C, at pH 7.5 and 25°C Escherichia coli
1.1.1.42 2100
-
 isocitrate wild type enzyme, at pH 7.5 and 25°C Escherichia coli