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Literature summary for 1.1.1.41 extracted from

  • Lin, A.P.; McAlister-Henn, L.
    Basis for half-site ligand binding in yeast NAD+-specific isocitrate dehydrogenase (2011), Biochemistry, 50, 8241-8250.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
AMP allosteric activation, isocitrate binding is essential for binding of AMP to IDH1 subunits Saccharomyces cerevisiae
AMP four AMP binding sites located on subunit IDH2 Saccharomyces cerevisiae
DTT
-
Saccharomyces cerevisiae
DTT decreases disulfide content of the enzyme, kinetics of enzyme mutants in presence or absence of DTT, overview Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged enzyme expression in Escherichia coli strain BL21-Gold(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C150S an octameric IDH1/IDH2C150S mutant enzyme, that shows unaltered activity and similar kinetics compared to the wild-type enzyme Saccharomyces cerevisiae
C150S site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme Saccharomyces cerevisiae
C56S/C150S/C242S site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme Saccharomyces cerevisiae
C56S/C242S an octameric IDH1/IDH2C56S/C242S mutant enzyme, the mutant enzyme shows a reduction in Vmax relative to that of the wild-type enzyme of about 50%, although about 30% activity is restored in the presence of dithiothreitol Saccharomyces cerevisiae
C56S/C242S site-directed mutagenesis, IDH1/IDH2C150S octameric enzyme Saccharomyces cerevisiae
G15D a tetrameric IDH1G15D/IDH2 mutant enzyme, that shows reduced activity and altered kinetics compared to the wild-type enzyme Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
Diamide increases disulfide content of the enzyme Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information NAD+-specific D-isocitrate dehydrogenase is an allosterically regulated. AMP and NAD+ binding kinetics of enzyme mutants in presence or absence of DTT, overview Saccharomyces cerevisiae
additional information
-
additional information yeast NAD+-specific isocitrate dehydrogenase is an allosterically regulated Saccharomyces cerevisiae
0.09
-
D-isocitrate octameric wild-type enzyme with AMP, without DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.1
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C150S with AMP, with or without DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.1
-
D-isocitrate octameric wild-type enzyme with AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.17
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP, without DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.19
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.2
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.32
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP, without DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.48
-
D-isocitrate octameric enzyme IDH1G15D/IDH2 with AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.5
-
D-isocitrate octameric enzyme IDH1G15D/IDH2 with AMP, without DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.51
-
D-isocitrate octameric wild-type enzyme without AMP, with DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.53
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C150S without AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.54
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C150S without AMP, with DTT, pH 7.4, 24°C Saccharomyces cerevisiae
0.56
-
D-isocitrate octameric wild-type enzyme without AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
1.01
-
D-isocitrate octameric enzyme mutant IDH1G15D/IDH2 without AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae
1.03
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S without AMP, with or without DTT, pH 7.4, 24°C Saccharomyces cerevisiae
1.19
-
D-isocitrate octameric enzyme IDH1G15D/IDH2 without AMP, with DTT, pH 7.4, 24°C Saccharomyces cerevisiae
1.3
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP, with DTT, pH 7.4, 24°C Saccharomyces cerevisiae
1.6
-
D-isocitrate octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP and DTT, pH 7.4, 24°C Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, activates Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37755
-
4 * 38001, subunit IDH1, + 4 * 37755, subunit IDH2, sequence calculation Saccharomyces cerevisiae
38001
-
4 * 38001, subunit IDH1, + 4 * 37755, subunit IDH2, sequence calculation Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-isocitrate + NAD+ Saccharomyces cerevisiae
-
2-oxoglutarate + CO2 + NADH
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21-Gold(DE3) by nickel affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-isocitrate + NAD+
-
Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH
-
?

Subunits

Subunits Comment Organism
More the enzyme is composed of four heterodimers, in two heterotetramers, of a catalytic IDH2 subunit and a regulatory IDH1 subunit, IDH octamer structure, overview Saccharomyces cerevisiae
octamer 4 * 38001, subunit IDH1, + 4 * 37755, subunit IDH2, sequence calculation Saccharomyces cerevisiae
octamer the enzyme is composed of four heterodimers of a catalytic IDH2 subunit and a regulatory IDH1 subunit Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
NAD+-specific isocitrate dehydrogenase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
24
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on, one NAD+ site per enzyme tetramer, two functional NAD+ binding sites in the wild-type enzyme Saccharomyces cerevisiae
NAD+ two NAD+ binding sites located on subunit IDH2 Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information interactions between sulfhydryl side chains of IDH2 Cys150 residues limit access to eight D-isocitrate and four AMP binding sites. In the presence of dithiothreitol, all ligand binding sites except for two potential NAD+ sites can be occupied Saccharomyces cerevisiae
additional information the IDH2 Cys-150 residue controls access to isocitrate binding sites. The wild-type enzyme displays four binding sites for isocitrate and two binding sites for AMP in the absence of dithiothreitol, and these numbers increase to eight and four in the presence of dithiothreitol, respectively Saccharomyces cerevisiae