EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.87 | acetate | slight inhibition | Saccharomyces cerevisiae | |
1.1.1.87 | Cl- | - |
Saccharomyces cerevisiae | |
1.1.1.87 | additional information | product and dead-end inhibition studies in the absence of K+ | Saccharomyces cerevisiae | |
1.1.1.87 | NAD+ | substrate inhibition at high concentrations and in absence of K+, kinetics, overview | Saccharomyces cerevisiae | |
1.1.1.286 | 3-carboxypropylidenemalate | - |
Saccharomyces cerevisiae | |
1.1.1.286 | Cl- | - |
Saccharomyces cerevisiae | |
1.1.1.286 | NADH | product inhibitor | Saccharomyces cerevisiae | |
1.1.1.286 | potassium acetate | - |
Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.87 | additional information | - |
additional information | substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl-, kinetic analysis, overview | Saccharomyces cerevisiae | |
1.1.1.87 | 0.3 | - |
NAD+ | pH 8.0, 25°C, in presence of K+ | Saccharomyces cerevisiae | |
1.1.1.87 | 9 | - |
NAD+ | pH 8.0, 25°C, in absence of K+ | Saccharomyces cerevisiae |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.87 | K+ | activates | Saccharomyces cerevisiae | |
1.1.1.87 | Mg2+ | activates, increase in the affinity of enzyme for Mg-HIc as a result of elimination of the inhibitory effect of Cl- | Saccharomyces cerevisiae | |
1.1.1.87 | additional information | selectivity of the activator site for monovalent ions, K+ is the best activator, and NH4+ and Rb+ are also activators of the reaction, while Cs+, Li+, and Na+ are not, overview. Substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+ | Saccharomyces cerevisiae | |
1.1.1.87 | NH4+ | activates | Saccharomyces cerevisiae | |
1.1.1.87 | Rb+ | activates | Saccharomyces cerevisiae | |
1.1.1.286 | K+ | best activator, 200 mM activates by 100%, increases the affinity of enzyme for NAD+ at high pH | Saccharomyces cerevisiae | |
1.1.1.286 | additional information | 200 mM Cs+, Li+, and Na+ do not activate | Saccharomyces cerevisiae | |
1.1.1.286 | NH4+ | 200 mM activates by 80.9% | Saccharomyces cerevisiae | |
1.1.1.286 | Rb+ | 200 mM activates by 29.3% | Saccharomyces cerevisiae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | Saccharomyces cerevisiae | - |
2-oxoadipate + NADH + H+ + CO2 | - |
? | |
1.1.1.286 | homoisocitrate + NAD+ | Saccharomyces cerevisiae | - |
? + NADH | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.87 | Saccharomyces cerevisiae | - |
- |
- |
1.1.1.286 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | - |
Saccharomyces cerevisiae | 2-oxoadipate + NADH + H+ + CO2 | - |
? | |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | substitution of potassium acetate for KCl changes the kinetic mechanism of HIcDH from a steady state random to a fully ordered mechanism with the binding of Mg-HIc followed by K+ and NAD+ | Saccharomyces cerevisiae | 2-oxoadipate + NADH + H+ + CO2 | - |
? | |
1.1.1.87 | isocitrate + NAD+ | low activity | Saccharomyces cerevisiae | ? + NADH + H+ | - |
? | |
1.1.1.286 | homoisocitrate + NAD+ | - |
Saccharomyces cerevisiae | ? + NADH | - |
? | |
1.1.1.286 | isocitrate + NAD+ | slow substrate | Saccharomyces cerevisiae | 2-oxoglutarate + CO2 + NADH + H+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.87 | HIc | - |
Saccharomyces cerevisiae |
1.1.1.87 | HIc dehydrogenase | - |
Saccharomyces cerevisiae |
1.1.1.87 | HICDH | - |
Saccharomyces cerevisiae |
1.1.1.286 | HICDH | - |
Saccharomyces cerevisiae |
1.1.1.286 | homoisocitrate dehydrogenase | - |
Saccharomyces cerevisiae |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.87 | 25 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.87 | 8 | - |
assay at | Saccharomyces cerevisiae |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.87 | additional information | - |
pH-rate profile in the absence of K+, overview | Saccharomyces cerevisiae |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.87 | NAD+ | - |
Saccharomyces cerevisiae | |
1.1.1.286 | NAD+ | - |
Saccharomyces cerevisiae |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.87 | 77 | - |
NAD+ | pH 8.0, 25°C, in absence of KOAc | Saccharomyces cerevisiae | |
1.1.1.286 | 2.7 | - |
NADH | - |
Saccharomyces cerevisiae | |
1.1.1.286 | 90 | - |
Cl- | - |
Saccharomyces cerevisiae | |
1.1.1.286 | 500 | - |
potassium acetate | - |
Saccharomyces cerevisiae |