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Literature summary for 1.1.1.42 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)

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

Protein Variants

Protein Variants Comment Organism
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
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]

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P08200
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Escherichia coli

kcat/KM [mM/s]

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