EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
- |
Thermus thermophilus |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
- |
Saccharomyces cerevisiae |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
strict specificity for homoisocitrate |
Candida albicans |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
i.e. (2R,3S)-homoisocitrate |
Thermus thermophilus |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex |
Candida albicans |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
- |
Saccharomyces cerevisiae ATCC 204508 |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
strict specificity for homoisocitrate |
Candida albicans ATCC 10231 |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
1.1.1.87 | (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ |
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex |
Candida albicans ATCC 10231 |
2-oxoadipate + CO2 + NADH + H+ |
- |
? |
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+ |
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 |
- |
? |