1.1.1.87: homoisocitrate dehydrogenase
This is an abbreviated version!
For detailed information about homoisocitrate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.87
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1.1.1.87
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alpha-aminoadipate
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3-isopropylmalate
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homocitrate
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homoaconitase
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beta-decarboxylating
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alpha-ketoadipate
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medicine
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synthesis
- 1.1.1.87
- alpha-aminoadipate
- 3-isopropylmalate
- homocitrate
- homoaconitase
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beta-decarboxylating
- alpha-ketoadipate
- medicine
- synthesis
Reaction
Synonyms
(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating), 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), beta-decarboxylating dehydrogenase, dehydrogenase, homoisocitrate, EC 1.1.1.155, HIc, HIc dehydrogenase, HICDH, homoisocitrate dehydrogenase, homoisocitric dehydrogenase, isocitrate-homoisocitrate dehydrogenase, LYS12, protein PH1722, ScHICDH, TK0280
ECTree
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Substrates Products
Substrates Products on EC 1.1.1.87 - homoisocitrate dehydrogenase
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REACTION DIAGRAM
2(R),3(S)-homoisocitrate + NAD+
alpha-ketoadipate + NADH + CO2 + H+
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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
-
-
?
homoisocitrate + NADP+
alpha-ketoadipate + NADPH + H+ + CO2
-
-
-
-
r
threo-D-isocitric acid + NAD+
?
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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
-
-
?
trisodium (2S,3R)-2-(carboxylatomethoxy)-3-hydroxybutanedioate + NAD+
? + NADH + CO2
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-
-
-
?
trisodium (2S,3R)-2-[(carboxylatomethyl)amino]-3-hydroxybutanedioate + NAD+
? + NADH + CO2
-
-
-
-
?
2-oxoadipate + CO2 + NADH + H+
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strict specificity for homoisocitrate
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-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
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strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
strict specificity for homoisocitrate, the enzyme selectively binds the Mg(II):homoisocitrate complex
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
i.e. (2R,3S)-homoisocitrate
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-
?
2-oxoadipate + NADH + H+ + CO2
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-
-
-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
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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
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-
?
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + NADH + H+ + CO2
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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+
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-
?
?
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more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate
-
-
?
1-hydroxy-1,2,3-propanetricarboxylate + NAD+
?
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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more effective substrate than 1-hydroxy-1,2,4-butanetricarboxylate
-
-
?
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
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-
-
-
r
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
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i.e. homoisocitrate
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r
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Saccharomycopsis lipolytica
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-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Saccharomycopsis lipolytica
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production of 2-oxoadipic acid, a precursor of lysine biosynthesis
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-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
alpha-aminoadipate pathway for biosynthesis of lysine
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
-
involved in lysine biosynthesis through alpha-aminoadipate
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
2-oxoadipate + CO2 + NADH
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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involved in lysine biosynthesis through alpha-aminoadipate
-
-
?
2-oxoadipate + CO2 + NADH
-
-
-
-
?
3-carboxy-2-hydroxyadipate + NAD+
2-oxoadipate + CO2 + NADH
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intermediate in lysine biosynthesis
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-
?
alpha-ketoisocaproate + NADH + H+ + CO2
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the enzyme has low catalytic efficiency toward 3-isopropylmalate
-
-
?
3-isopropylmalate + NAD+
alpha-ketoisocaproate + NADH + H+ + CO2
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the enzyme has low catalytic efficiency toward 3-isopropylmalate
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-
?
alpha-ketoadipate + NADH + H+ + CO2
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highest activity
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-
r
homoisocitrate + NAD+
alpha-ketoadipate + NADH + H+ + CO2
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highest activity
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r
isocitrate + NADP+
2-oxoglutarate + NADPH + H+ + CO2
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-
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?
additional information
?
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retinol dehydrogenase 10 activity is critical for spatiotemporal synthesis of retinoic acid during embrogenesis
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?
additional information
?
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the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway
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?
additional information
?
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the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway
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?
additional information
?
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catalyzes keto-enol tautomerization of tritiated alpha-ketoadipate, not: ethanol, isocitrate, malate, glutamate
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?
additional information
?
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no activity with isocitrate, isopropylmalate, and tartrate
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-
?
additional information
?
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the wild-type enzyme with isocitrate as the substrate is about 200times slower than with homoisocitrate
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-
?
additional information
?
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the wild-type enzyme with isocitrate as the substrate is about 200times slower than with homoisocitrate
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-
?
additional information
?
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no activity with L-tartrate
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-
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additional information
?
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substrate binding site structure, the substrate specificity is determined by residue Arg85, no activity with 3-isopropylmalate
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-
?
additional information
?
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Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
no activity with 3-isopropylmalate
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-
?