Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-carboxypropylidenemalate | - |
Saccharomyces cerevisiae | |
Mg-homoisocitrate | - |
Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0042 | - |
homoisocitrate | oxidate decarboxylation of homoisocitrate | Saccharomyces cerevisiae | |
0.09 | - |
NADH | reductive carboxylation of alpha-ketoadipate | Saccharomyces cerevisiae | |
0.45 | - |
NAD+ | oxidate decarboxylation of homoisocitrate | Saccharomyces cerevisiae | |
3.2 | - |
homoisocitrate | reductive carboxylation of alpha-ketoadipate | Saccharomyces cerevisiae | |
16.3 | - |
CO2 | reductive carboxylation of alpha-ketoadipate | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Saccharomyces cerevisiae |
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+ | two enzyme groups act as acid-base catalysts in the reaction. A group with a pKa of 6.5-7 acts as a general base accepting a proton as the beta-hydroxy acid is oxidized to the beta-keto acid, and this residue participates in all three of the chemical steps, acting to shuttle a proton between the C2 hydroxyl and itself. The second group acts as a general acid with a pKa of 9.5 and likely catalyzes the tautomerization step by donating a proton to the enol to give the final product | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2(R),3(S)-homoisocitrate + NAD+ | with homoisocitrate as the substrate, no primary deuterium isotope effect is observed, and a small 13C kinetic isotope effect indicates that the decarboxylation step contributes only slightly to rate limitation | Saccharomyces cerevisiae | alpha-ketoadipate + NADH + CO2 + H+ | - |
? | |
homoisocitrate + NAD+ | - |
Saccharomyces cerevisiae | alpha-ketoadipate + NADH + CO2 + H+ | - |
r | |
homoisocitrate + NAD+ | - |
Saccharomyces cerevisiae | 2-oxoadipate + CO2 + NADH + H+ | - |
r | |
isocitrate + NAD+ | - |
Saccharomyces cerevisiae | ? | - |
r | |
threo-D-isocitric acid + NAD+ | with isocitrate as the substrate, primary deuterium and 13C isotope effects indicate that hydride transfer and decarboxylation steps contribute to rate limitation, and that the decarboxylation step is the more rate-limiting of the two. The multiple-substrate deuterium/13C isotope effects suggest a stepwise mechanism with hydride transfer preceding decarboxylation | Saccharomyces cerevisiae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
3-carboxy-2-hydroxyadipate dehydrogenase | - |
Saccharomyces cerevisiae |
HICDH | - |
Saccharomyces cerevisiae |
homoisocitrate dehydrogenase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
7 | - |
reductive carboxylation | Saccharomyces cerevisiae |
7.5 | - |
oxidative decarboxylation | Saccharomyces cerevisiae |
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharomyces cerevisiae |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
enzyme is stable when incubated for at least 15 min over the pH range of 5.0-10.0 | Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.002 | - |
Mg-homoisocitrate | oxidate decarboxylation of homoisocitrate | Saccharomyces cerevisiae |