Protein Variants | Comment | Organism |
---|---|---|
K206M | site-directed mutagenesis, the active site mutant shows about 2400fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly | Saccharomyces cerevisiae |
Y150F | site-directed mutagenesis, the active site mutant shows about 680fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | mutant enzymes kinetic analysis and pH-dependencies, overview | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | dependent on | Saccharomyces cerevisiae | |
Mg2+ | dependent on | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | Saccharomyces cerevisiae | - |
2-oxoadipate + NADH + H+ + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | - |
Saccharomyces cerevisiae | 2-oxoadipate + NADH + H+ + CO2 | - |
? | |
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | homoisocitrate dehydrogenase catalyzes the Mg2+- and K+-dependent oxidative decarboxylation of homoisocitrate to alpha-ketoadipate using NAD as the oxidant, it utilizes a Lys-Tyr pair to catalyze the acid-base chemistry of the reaction, the active site Lys-Tyr pair consists of lysine 206 and tyrosine 150 | Saccharomyces cerevisiae | 2-oxoadipate + NADH + H+ + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HIc dehydrogenase | - |
Saccharomyces cerevisiae |
HICDH | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
mutant enzymes kinetics and pH-dependencies, overview | Saccharomyces cerevisiae |
7.5 | - |
assay at | Saccharomyces cerevisiae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.2 | 9.5 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Saccharomyces cerevisiae |