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Literature summary 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.41 | expressed in Escherichia coli strain BL21-CodonPlus (DE3)-RIL | Pyrococcus horikoshii |
| 1.1.1.87 | DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli | Pyrococcus horikoshii |
| 1.1.1.286 | - |
Pyrococcus horikoshii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.41 | 0.0164 | - |
isocitrate | 6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1mM NAD+ | Pyrococcus horikoshii |  |
| 1.1.1.41 | 0.0183 | - |
homoisocitrate | 6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1mM NAD+ | Pyrococcus horikoshii | |
| 1.1.1.41 | 0.0771 | - |
NAD+ | 6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2 | Pyrococcus horikoshii | |
| 1.1.1.87 | 0.0164 | - |
isocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
| 1.1.1.87 | 0.0183 | - |
homoisocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
| 1.1.1.286 | 0.0164 | - |
isocitrate | 70°C, pH 7.8 | Pyrococcus horikoshii | |
| 1.1.1.286 | 0.0183 | - |
homoisocitrate | 70°C, pH 7.8 | Pyrococcus horikoshii | |
| 1.1.1.286 | 0.0771 | - |
NAD+ | 70°C, pH 7.8 | Pyrococcus horikoshii | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.41 | K+ | - |
Pyrococcus horikoshii | |
| 1.1.1.41 | Mn2+ | - |
Pyrococcus horikoshii | |
| 1.1.1.87 | Mn2+ | - |
Pyrococcus horikoshii | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.87 | 3-isopropylmalate + NAD+ | Pyrococcus horikoshii | - |
? | - |
? | |
| 1.1.1.87 | homoisocitrate + NAD+ | Pyrococcus horikoshii | - |
? | - |
? | |
| 1.1.1.87 | isocitrate + NAD+ | Pyrococcus horikoshii | - |
? | - |
? | |
| 1.1.1.87 | additional information | Pyrococcus horikoshii | the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.41 | Pyrococcus horikoshii | - |
- |
- |
| 1.1.1.87 | Pyrococcus horikoshii | A4CYJ9 | gene PH1722 or hdh | - |
| 1.1.1.286 | Pyrococcus horikoshii | - |
expression in Escherichia coli | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.41 | Hi-Trap chelating HP column chromatography | Pyrococcus horikoshii |
| 1.1.1.87 | recombinnat His-tagged enzyme from Escherichia coli by metal affinity chromatography | Pyrococcus horikoshii |
| 1.1.1.286 | recombinant enzyme expressed in Escherichia coli, purification of inclusion bodies requires N-laurylsarcosine | Pyrococcus horikoshii |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.1.1.41 | using N-lauroylsarcosine to 0.3% v/v | Pyrococcus horikoshii |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.41 | additional information | - |
no activity on 3-isopropylmalate | Pyrococcus horikoshii |
| 1.1.1.87 | additional information | - |
- |
Pyrococcus horikoshii |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.41 | D-homoisocitrate + NAD+ | - |
Pyrococcus horikoshii | ? + NADH | - |
? | |
| 1.1.1.41 | D-isocitrate + NAD+ | - |
Pyrococcus horikoshii | 2-oxoglutarate + CO2 + NADH | - |
? | |
| 1.1.1.41 | isocitrate + NAD+ | - |
Pyrococcus horikoshii | 2-oxoglutarate + CO2 + NADH + H+ | - |
r | |
| 1.1.1.87 | 3-isopropylmalate + NAD+ | - |
Pyrococcus horikoshii | ? | - |
? | |
| 1.1.1.87 | homoisocitrate + NAD+ | - |
Pyrococcus horikoshii | ? | - |
? | |
| 1.1.1.87 | isocitrate + NAD+ | - |
Pyrococcus horikoshii | ? | - |
? | |
| 1.1.1.87 | additional information | the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway | Pyrococcus horikoshii | ? | - |
? | |
| 1.1.1.286 | homoisocitrate + NAD+ | - |
Pyrococcus horikoshii | ? + NADH | - |
? | |
| 1.1.1.286 | isocitrate + NAD+ | about 20times more efficient than homoisocitrate, NAD+ is preferred over NADP+ | Pyrococcus horikoshii | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
| 1.1.1.286 | isocitrate + NADP+ | NAD+ is preferred over NADP+ | Pyrococcus horikoshii | 2-oxoglutarate + CO2 + NADPH + H+ | - |
? | |
| 1.1.1.286 | additional information | no substrate: 3-isopropylmalate | Pyrococcus horikoshii | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.41 | beta-decarboxylating dehydrogenase | - |
Pyrococcus horikoshii |
| 1.1.1.41 | isocitrate-homoisocitrate dehydrogenase | - |
Pyrococcus horikoshii |
| 1.1.1.41 | PH1722 | - |
Pyrococcus horikoshii |
| 1.1.1.87 | HICDH | - |
Pyrococcus horikoshii |
| 1.1.1.87 | isocitrate-homoisocitrate dehydrogenase | - |
Pyrococcus horikoshii |
| 1.1.1.87 | protein PH1722 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.87 | 70 | - |
assay at | Pyrococcus horikoshii |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.41 | 13.7 | - |
homoisocitrate | 6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1 mM NAD+ | Pyrococcus horikoshii | |
| 1.1.1.41 | 14.8 | - |
isocitrate | 6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2, 1 mM NAD+ | Pyrococcus horikoshii | |
| 1.1.1.41 | 21.8 | - |
NAD+ | 6fold His-tagged enzyme, at 70°C in 50 mM N-2-hydroxyethylpiperadine-N0-2-ethanesulfonate-NaOH (pH 7.8), 0.2 M KCl, 0.2 mM MnCl2 | Pyrococcus horikoshii | |
| 1.1.1.87 | 13.7 | - |
homoisocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
| 1.1.1.87 | 14.8 | - |
isocitrate | pH 7.8, 70°C, recombinant enzyme | Pyrococcus horikoshii | |
| 1.1.1.286 | 13.7 | - |
homoisocitrate | 70°C, pH 7.8 | Pyrococcus horikoshii | |
| 1.1.1.286 | 14.8 | - |
isocitrate | 70°C, pH 7.8 | Pyrococcus horikoshii | |
| 1.1.1.286 | 21.8 | - |
NAD+ | 70°C, pH 7.8 | Pyrococcus horikoshii | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.87 | 7.8 | - |
assay at | Pyrococcus horikoshii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.41 | NAD+ | 1 mM | Pyrococcus horikoshii | |
| 1.1.1.87 | NAD+ | - |
Pyrococcus horikoshii | |
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Release 2023.1 (January 2023)
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