EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.42 | additional information | glucose induces epression of isozyme IDP1, glycerol induces epression of isozymes IDP1 and IDP2, fatty acids induce epression of isozymes IDP1, IDP2, and IDP3 | Saccharomyces cerevisiae |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.42 | expression of C-terminally His-tagged enzyme in Escherichia coli BL21(DE3) | Homo sapiens |
1.1.1.42 | expression of isozyme IDP1 and IDP2 as His-tagged enzymes in a disruption mutant | Saccharomyces cerevisiae |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.42 | hanging drop vapour diffusion method, purified recombinant His-tagged enzyme in complex with NADP+: equal volume of protein solution, containing 15 mg/ml enzyme, 20 mM Tris-HCl, pH 7.4, 100 mM NaCl, and 10 mM NADP+, and of reservoir solution, containing 100 mM MES, pH 6.5, 12% PEG 20000, at 4°C, purified recombinant His-tagged enzyme in complex with NADP+, isocitrate and Ca2+: equal volume of protein solution, containing 15 mg/ml enzyme, 20 mM Tris-HCl, pH 7.4, 100 mM NaCl, and 10 mM NADP+, 10 mM DL-isocitrate and 10 mM CaCl2, and of reservoir solution, containing 100 mM MES, pH 5.9, 20% PEG 6000, at 20°C, X-ray diffraction structure determination and analysis | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.42 | additional information | - |
additional information | kinetics of isozymes IDP1 and IDP2 | Saccharomyces cerevisiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.1.1.42 | cytosol | - |
Homo sapiens | 5829 | - |
1.1.1.42 | cytosol | isozyme IDP2 | Saccharomyces cerevisiae | 5829 | - |
1.1.1.42 | mitochondrion | isozyme IDP1 | Saccharomyces cerevisiae | 5739 | - |
1.1.1.42 | peroxisome | isoyzme IDP3 | Saccharomyces cerevisiae | 5777 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.42 | Ca2+ | divalent metal ion is required, binding structure and conformation at the isocitrate-metal-binding site | Homo sapiens | |
1.1.1.42 | Mg2+ | - |
Saccharomyces cerevisiae | |
1.1.1.42 | Mg2+ | divalent metal ion is required, binding structure and conformation at the isocitrate-metal-binding site | Homo sapiens |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.42 | 46381 | - |
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry | Saccharomyces cerevisiae |
1.1.1.42 | 46562 | - |
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry | Saccharomyces cerevisiae |
1.1.1.42 | 47856 | - |
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.42 | D-isocitrate + NADP+ | Saccharomyces cerevisiae | the reaction is reversible for isozyme IDP2 | 2-oxoglutarate + CO2 + NADPH | - |
r | |
1.1.1.42 | isocitrate + NADP+ | Homo sapiens | enzyme has a self-regulatory mechanism of activity mimicking the phosphorylation mechanism of bacterial enzymes | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.42 | Homo sapiens | - |
- |
- |
1.1.1.42 | Saccharomyces cerevisiae | - |
1 cytosolic, 1 peroxisomal, and 1 mitochondrial isozyme | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.42 | recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Homo sapiens |
1.1.1.42 | recombinant His-tagged isozymes IDP1 and IDP2 by nickel affinity chromatography | Saccharomyces cerevisiae |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.1.42 | isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ | active site structure and reaction mechanism, conformational changes at the active site resulting in closed and open forms, regulatory residues are isocitrate-binding Asp279and Ser94 | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.42 | D-isocitrate + NADP+ | the reaction is reversible for isozyme IDP2 | Saccharomyces cerevisiae | 2-oxoglutarate + CO2 + NADPH | - |
r | |
1.1.1.42 | isocitrate + NADP+ | - |
Homo sapiens | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
1.1.1.42 | isocitrate + NADP+ | enzyme has a self-regulatory mechanism of activity mimicking the phosphorylation mechanism of bacterial enzymes | Homo sapiens | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.42 | ? | x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry | Saccharomyces cerevisiae |
1.1.1.42 | More | enzyme has 3 different conformational stages | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.42 | IDP | - |
Saccharomyces cerevisiae |
1.1.1.42 | NADP-dependent isocitrate dehydrogenase | - |
Homo sapiens |
1.1.1.42 | NADP-dependent isocitrate dehydrogenase | - |
Saccharomyces cerevisiae |
1.1.1.42 | NADP-IDH | - |
Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.42 | 6.5 | - |
assay at, reverse reaction | Saccharomyces cerevisiae |
1.1.1.42 | 7.4 | - |
assay at | Homo sapiens |
1.1.1.42 | 7.5 | - |
isozyme IDP2, forward reaction | Saccharomyces cerevisiae |
1.1.1.42 | 8 | - |
isozyme IDP1, forward reaction | Saccharomyces cerevisiae |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.42 | 6 | 9.5 | - |
Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.42 | NADP+ | - |
Saccharomyces cerevisiae | |
1.1.1.42 | NADP+ | binding site structure, interaction with the 2'-phosphate group of the ribose moiety | Homo sapiens | |
1.1.1.42 | NADPH | - |
Saccharomyces cerevisiae |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.1.1.42 | Saccharomyces cerevisiae | isozyme IDP2 | - |
5.5 |
1.1.1.42 | Saccharomyces cerevisiae | isozyme IDP1 | - |
8.5 |
1.1.1.42 | Saccharomyces cerevisiae | isozyme IDP3 | - |
10 |