EC 1.1.1.286: isocitrate-homoisocitrate dehydrogenase
This is an abbreviated version!
For detailed information about isocitrate-homoisocitrate dehydrogenase, go to the full flat file.
Reaction
Synonyms
3-carboxy-2-hydroxyadipate dehydrogenase, HICDH, homoisocitrate dehydrogenase, isocitrate-homoisocitrate dehydrogenase, More, Saci_2375, TK0280
ECTree
1.1.1.286 isocitrate-homoisocitrate dehydrogenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.1.1.286 - isocitrate-homoisocitrate dehydrogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY 
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+
2-oxoadipate + CO2 + NADH + H+
-
Substrates: chemical mechanism, stereochemistry of hydride transfer to NAD, overview
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?
3-isopropylmalate + NAD+
?
-
Substrates: at 0.1% of the rate with homoisocitrate
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?
3-isopropylmalate + NAD+
2-oxoisocaproate + CO2 + NADH + H+
Substrates: -
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?
3-isopropylmalate + NAD+
2-oxoisocaproate + CO2 + NADH + H+
Substrates: -
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?
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
Substrates: -
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?
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
Substrates: -
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?
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
Substrates: -
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r
homoisocitrate + NAD+
2-oxoadipate + CO2 + NADH + H+
Substrates: -
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r
homoisocitrate + NAD+
? + NADH
-
Substrates: 1.5fold preferred over isocitrate
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?
homoisocitrate + NAD+
? + NADH
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: -
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?
homoisocitrate + NADP+
2-oxoadipate + CO2 + NADPH + H+
Substrates: -
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r
homoisocitrate + NADP+
2-oxoadipate + CO2 + NADPH + H+
Substrates: -
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r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
Substrates: -
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
Substrates: about 20times more efficient than homoisocitrate, NAD+ is preferred over NADP+
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
Substrates: rapid equilibrium random catalytic mechanism, stereochemistry of hydride transfer to NAD, overview
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
-
Substrates: slow substrate
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Substrates: -
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Substrates: -
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Substrates: about 20times more efficient than homoisocitrate
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?
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Substrates: -
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r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Substrates: -
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r
isocitrate + NAD+
2-oxoglutarate + CO2 + NADH + H+
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: about 20times more efficient than homoisocitrate
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
Substrates: NAD+ is preferred over NADP+
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
-
Substrates: NAD+ is preferred over NADP+
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?
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
Substrates: -
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r
isocitrate + NADP+
2-oxoglutarate + CO2 + NADPH + H+
Substrates: -
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r
additional information
?
-
-
Substrates: no substrate: NADP+
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?
additional information
?
-
-
Substrates: no substrate: 3-isopropylmalate
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?
additional information
?
-
-
Substrates: 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
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?
additional information
?
-
Substrates: Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
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?
additional information
?
-
-
Substrates: Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
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?
additional information
?
-
Substrates: Saci_2375 exhibits distinct and similar activities for isocitrate and homoisocitrate, but no detectable activity for 3-isopropylmalate. Saci_2375 is a dual function enzyme serving as isocitrate-homoisocitrate dehydrogenase
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?
additional information
?
-
Substrates: residues Thr71 and Ser80 play important roles in the recognition of homoisocitrate and isocitrate while the hydrophobic region consisting of Ile82 and Leu83 is responsible for the recognition of 3-isopropylmalate. Importance of a water-mediated hydrogen bond network for the stabilization of the beta3-alpha4 loop, including the Thr71 residue, with respect to the promiscuity of the substrate specificity of TK0280
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?
additional information
?
-
Substrates: residues Thr71 and Ser80 play important roles in the recognition of homoisocitrate and isocitrate while the hydrophobic region consisting of Ile82 and Leu83 is responsible for the recognition of 3-isopropylmalate. Importance of a water-mediated hydrogen bond network for the stabilization of the beta3-alpha4 loop, including the Thr71 residue, with respect to the promiscuity of the substrate specificity of TK0280
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?
additional information
?
-
Substrates: no substrate: 3-isopropylmalate
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?
additional information
?
-
Substrates: in contrast to other homoisicitrate dehydrogenases, the homoisocitrate dehydrogenase from the thermophilic bacterium Thermus thermophilus (TtHICDH) catalyzes the reactions using both homoisocitrate and isocitrate as substrates at similar efficiencies
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?
additional information
?
-
Substrates: dual substrate specificity for homoisocitrate dehydrogenase
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?
additional information
?
-
Substrates: in contrast to other homoisicitrate dehydrogenases, the homoisocitrate dehydrogenase from the thermophilic bacterium Thermus thermophilus (TtHICDH) catalyzes the reactions using both homoisocitrate and isocitrate as substrates at similar efficiencies
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?
additional information
?
-
Substrates: dual substrate specificity for homoisocitrate dehydrogenase
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?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: no substrate: 3-isopropylmalate
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?
