Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-carboxypropylidenemalate | a dead-end inhibitor, competitive versus homoisocitrate | Saccharomyces cerevisiae | |
homoisocitrate | competitive, pH-dependent substrate inhibition | Saccharomyces cerevisiae | |
isocitrate | competitive, pH-dependent substrate inhibition | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic mechanism, detailed overview | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | the enzyme catalyzes the fourth reaction of the alpha-aminoadipate pathway for lysine biosynthesis, the conversion of homoisocitrate to alpha-ketoadipate using NAD+ as an oxidizing agent | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+ | chemical mechanism on the basis of the pH dependence of kinetic parameters, dissociation constants for competitive inhibitors, and multiple-substrate deuterium/13C isotope effects suggesting a stepwise mechanism with hydride transfer preceding decarboxylation, the decarboxylation step contributes only slightly to rate limitation, overview | Saccharomyces cerevisiae | |
isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH + H+ | chemical mechanism on the basis of the pH dependence of kinetic parameters, dissociation constants for competitive inhibitors, and multiple-substrate deuterium/13C isotope effects suggesting a stepwise mechanism with hydride transfer preceding decarboxylation, the decarboxylation step contributes only slightly to rate limitation, overview | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ | chemical mechanism, stereochemistry of hydride transfer to NAD, overview | Saccharomyces cerevisiae | 2-oxoadipate + CO2 + NADH + H+ | - |
? | |
isocitrate + NAD+ | rapid equilibrium random catalytic mechanism, stereochemistry of hydride transfer to NAD, overview | Saccharomyces cerevisiae | 2-oxoglutarate + CO2 + NADH + H+ | - |
? | |
additional information | the enzyme catalyzes the fourth reaction of the alpha-aminoadipate pathway for lysine biosynthesis, the conversion of homoisocitrate to alpha-ketoadipate using NAD+ as an oxidizing agent | Saccharomyces cerevisiae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-carboxy-2-hydroxyadipate dehydrogenase | - |
Saccharomyces cerevisiae |
HICDH | - |
Saccharomyces cerevisiae |
homoisocitrate dehydrogenase | - |
Saccharomyces cerevisiae |
More | HIcDH is a member of the family of pyridine nucleotide-linked beta-hydroxy acid oxidative decarboxylases | Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Saccharomyces cerevisiae |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 10 | pH-profile, overview | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | stereochemistry of hydride transfer to NAD, overview | Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.043 | - |
3-carboxypropylidenemalate | pH 8.0, 25°C, versus homoisocitrate | Saccharomyces cerevisiae |