1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ - Thermus thermophilus 2-oxoadipate + CO2 + NADH + H+ - ? 395041 1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ - Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH + H+ - ? 395041 1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ strict specificity for homoisocitrate Candida albicans 2-oxoadipate + CO2 + NADH + H+ - ? 395041 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+ - ? 395041 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+ - ? 395041 1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ - Saccharomyces cerevisiae ATCC 204508 2-oxoadipate + CO2 + NADH + H+ - ? 395041 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+ - ? 395041 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+ - ? 395041 1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ - Saccharomyces cerevisiae 2-oxoadipate + NADH + H+ + CO2 - ? 402274 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 - ? 402274 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 - ? 402274 1.1.1.87 (2R,3S)-3-(2-hydroxyethyl)malate + NAD+ - Saccharomyces cerevisiae ? - ? 383432 1.1.1.87 (2R,3S)-3-(2-hydroxyethyl)malate + NAD+ - Deinococcus radiodurans ? - ? 383432 1.1.1.87 (2R,3S)-3-(3-aminopropyl)malate + NAD+ - Saccharomyces cerevisiae ? - ? 383433 1.1.1.87 (2R,3S)-3-(3-aminopropyl)malate + NAD+ - Deinococcus radiodurans ? - ? 383433 1.1.1.87 (2R,3S)-3-(3-hydroxypropyl)malate + NAD+ - Saccharomyces cerevisiae ? - ? 383434 1.1.1.87 (2R,3S)-3-(3-hydroxypropyl)malate + NAD+ - Deinococcus radiodurans ? - ? 383434 1.1.1.87 (2R,3S)-3-(4-hydroxybutyl)malate + NAD+ - Saccharomyces cerevisiae ? - ? 383435 1.1.1.87 (2R,3S)-3-(4-hydroxybutyl)malate + NAD+ - Deinococcus radiodurans ? - ? 383435 1.1.1.87 (2R,3S)-3-(4-pentenyl)malic acid + NAD+ - Saccharomyces cerevisiae ? - ? 383436 1.1.1.87 (2R,3S)-3-(4-pentenyl)malic acid + NAD+ - Deinococcus radiodurans ? - ? 383436 1.1.1.87 (2R,3S)-3-allylmalic acid + NAD+ - Saccharomyces cerevisiae ? - ? 383437 1.1.1.87 (2R,3S)-3-allylmalic acid + NAD+ - Deinococcus radiodurans ? - ? 383437 1.1.1.87 (2R,3S)-3-propylmalic acid + NAD+ - Saccharomyces cerevisiae ? - ? 383438 1.1.1.87 (2R,3S)-3-propylmalic acid + NAD+ - Deinococcus radiodurans ? - ? 383438 1.1.1.87 1-hydroxy-1,2,3-propanetricarboxylate + NAD+ more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate Thermus thermophilus ? - ? 371493 1.1.1.87 1-hydroxy-1,2,3-propanetricarboxylate + NAD+ more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 ? - ? 371493 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Thermus thermophilus 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH - r 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Schizosaccharomyces pombe 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Candida albicans 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Cryptococcus neoformans 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Saccharomycopsis lipolytica 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Aspergillus fumigatus 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ i.e. homoisocitrate Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH - r 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ alpha-aminoadipate pathway for biosynthesis of lysine Schizosaccharomyces pombe 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ production of 2-oxoadipic acid, a precursor of lysine biosynthesis Saccharomycopsis lipolytica 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ involved in lysine biosynthesis through alpha-aminoadipate Thermus thermophilus 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ - Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 1-hydroxy-1,2,4-butanetricarboxylate + NAD+ involved in lysine biosynthesis through alpha-aminoadipate Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 2-oxoadipate + CO2 + NADH - ? 359216 1.1.1.87 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+ - ? 395334 1.1.1.87 3-carboxy-2-hydroxyadipate + NAD+ - Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH - ? 359218 1.1.1.87 3-carboxy-2-hydroxyadipate + NAD+ intermediate in lysine biosynthesis Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH - ? 359218 1.1.1.87 3-isopropylmalate + NAD+ - Deinococcus radiodurans ? - ? 379024 1.1.1.87 3-isopropylmalate + NAD+ - Pyrococcus horikoshii ? - ? 379024 1.1.1.87 3-isopropylmalate + NAD+ the enzyme has low catalytic efficiency toward 3-isopropylmalate Thermococcus kodakarensis alpha-ketoisocaproate + NADH + H+ + CO2 - ? 459035 1.1.1.87 3-isopropylmalate + NAD+ the enzyme has low catalytic efficiency toward 3-isopropylmalate Thermococcus kodakarensis KUW1 alpha-ketoisocaproate + NADH + H+ + CO2 - ? 459035 1.1.1.87 3-vinylmalate + NAD+ - Saccharomyces cerevisiae ? - ? 383859 1.1.1.87 3-vinylmalate + NAD+ - Deinococcus radiodurans ? - ? 383859 1.1.1.87 D-malate + NAD+ weak activity Thermococcus kodakarensis ? - ? 459591 1.1.1.87 D-malate + NAD+ weak activity Thermococcus kodakarensis KUW1 ? - ? 459591 1.1.1.87 ethylmalate + NAD+ - Saccharomyces cerevisiae ? - ? 384700 1.1.1.87 ethylmalate + NAD+ - Deinococcus radiodurans ? - ? 384700 1.1.1.87 homoisocitrate + NAD+ - Thermus thermophilus ? - ? 383196 1.1.1.87 homoisocitrate + NAD+ - Saccharomyces cerevisiae ? - ? 383196 1.1.1.87 homoisocitrate + NAD+ - Deinococcus radiodurans ? - ? 383196 1.1.1.87 homoisocitrate + NAD+ - Pyrococcus horikoshii ? - ? 383196 1.1.1.87 homoisocitrate + NAD+ 1.5fold preferred to isocitrate Deinococcus radiodurans ? - ? 383196 1.1.1.87 homoisocitrate + NAD+ - Saccharomyces cerevisiae alpha-ketoadipate + NADH + CO2 - r 397438 1.1.1.87 homoisocitrate + NAD+ - Saccharomyces cerevisiae alpha-ketoadipate + NADH + CO2 + H+ - r 397439 1.1.1.87 homoisocitrate + NAD+ - Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH + H+ - r 438359 1.1.1.87 homoisocitrate + NAD+ highest activity Thermococcus kodakarensis alpha-ketoadipate + NADH + H+ + CO2 - r 459746 1.1.1.87 homoisocitrate + NAD+ highest activity Thermococcus kodakarensis KUW1 alpha-ketoadipate + NADH + H+ + CO2 - r 459746 1.1.1.87 homoisocitrate + NADP+ - Thermococcus kodakarensis alpha-ketoadipate + NADPH + H+ + CO2 - r 459747 1.1.1.87 isocitrate + NAD+ - Saccharomyces cerevisiae ? - r 383218 1.1.1.87 isocitrate + NAD+ - Deinococcus radiodurans ? - ? 383218 1.1.1.87 isocitrate + NAD+ - Pyrococcus horikoshii ? - ? 383218 1.1.1.87 isocitrate + NAD+ 20fold preferred to homoisocitrate Thermus thermophilus ? - ? 383218 1.1.1.87 isocitrate + NAD+ low activity Saccharomyces cerevisiae ? + NADH + H+ - ? 405511 1.1.1.87 isocitrate + NADP+ - Thermococcus kodakarensis 2-oxoglutarate + NADPH + H+ + CO2 - ? 188124 1.1.1.87 isocitrate + NADP+ - Thermococcus kodakarensis KUW1 2-oxoglutarate + NADPH + H+ + CO2 - ? 188124 1.1.1.87 isopropylmalate + NAD+ - Deinococcus radiodurans ? - ? 257337 1.1.1.87 additional information catalyzes keto-enol tautomerization of tritiated alpha-ketoadipate, not: ethanol, isocitrate, malate, glutamate Saccharomyces cerevisiae ? - ? 89 1.1.1.87 additional information no activity with 3-isopropylmalate Thermus thermophilus ? - ? 89 1.1.1.87 additional information the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway Pyrococcus horikoshii ? - ? 89 1.1.1.87 additional information no activity with isocitrate, isopropylmalate, and tartrate Saccharomyces cerevisiae ? - ? 89 1.1.1.87 additional information no activity with tartrate Deinococcus radiodurans ? - ? 89 1.1.1.87 additional information substrate binding site structure, the substrate specificity is determined by residue Arg85, no activity with 3-isopropylmalate Thermus thermophilus ? - ? 89 1.1.1.87 additional information retinol dehydrogenase 10 activity is critical for spatiotemporal synthesis of retinoic acid during embrogenesis Mus musculus ? - ? 89 1.1.1.87 additional information substrate docking study Candida albicans ? - ? 89 1.1.1.87 additional information the wild-type enzyme with isocitrate as the substrate is about 200times slower than with homoisocitrate Saccharomyces cerevisiae ? - ? 89 1.1.1.87 additional information no activity with L-tartrate Thermococcus kodakarensis ? - - 89 1.1.1.87 additional information no activity with 3-isopropylmalate Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 ? - ? 89 1.1.1.87 additional information no activity with L-tartrate Thermococcus kodakarensis KUW1 ? - - 89 1.1.1.87 additional information substrate docking study Candida albicans ATCC 10231 ? - ? 89 1.1.1.87 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 ? - ? 398426 1.1.1.87 trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate + NAD+ - Saccharomyces cerevisiae ? + NADH + CO2 - ? 413002 1.1.1.87 trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate + NAD+ - Saccharomyces cerevisiae ? + NADH + CO2 - ? 413003