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Literature summary for 1.1.1.87 extracted from
- Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase (2005), Biochem. Biophys. Res. Commun., 331, 341-346.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli | Pyrococcus horikoshii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0164 | - |
isocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii |  |
| 0.0183 | - |
homoisocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mn2+ | - |
Pyrococcus horikoshii | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-isopropylmalate + NAD+ | Pyrococcus horikoshii | - |
? | - |
? | |
| homoisocitrate + NAD+ | Pyrococcus horikoshii | - |
? | - |
? | |
| isocitrate + NAD+ | Pyrococcus horikoshii | - |
? | - |
? | |
| additional information | Pyrococcus horikoshii | the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | A4CYJ9 | gene PH1722 or hdh | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinnat His-tagged enzyme from Escherichia coli by metal affinity chromatography | Pyrococcus horikoshii |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Pyrococcus horikoshii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-isopropylmalate + NAD+ | - |
Pyrococcus horikoshii | ? | - |
? | |
| homoisocitrate + NAD+ | - |
Pyrococcus horikoshii | ? | - |
? | |
| isocitrate + NAD+ | - |
Pyrococcus horikoshii | ? | - |
? | |
| additional information | the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway | Pyrococcus horikoshii | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HICDH | - |
Pyrococcus horikoshii |
| isocitrate-homoisocitrate dehydrogenase | - |
Pyrococcus horikoshii |
| protein PH1722 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
assay at | Pyrococcus horikoshii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 13.7 | - |
homoisocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
| 14.8 | - |
isocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
assay at | Pyrococcus horikoshii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Pyrococcus horikoshii | |
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Release 2023.1 (January 2023)
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