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Literature summary for 1.1.1.286 extracted from

  • Lin, Y.; Volkman, J.; Nicholas, K.M.; Yamamoto, T.; Eguchi, T.; Nimmo, S.L.; West, A.H.; Cook, P.F.
    Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae (2008), Biochemistry, 47, 4169-4180.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-carboxypropylidenemalate a dead-end inhibitor, competitive versus homoisocitrate Saccharomyces cerevisiae
homoisocitrate competitive, pH-dependent substrate inhibition Saccharomyces cerevisiae
isocitrate competitive, pH-dependent substrate inhibition Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanism, detailed overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-

Reaction

Reaction Comment Organism Reaction ID
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+ chemical mechanism on the basis of the pH dependence of kinetic parameters, dissociation constants for competitive inhibitors, and multiple-substrate deuterium/13C isotope effects suggesting a stepwise mechanism with hydride transfer preceding decarboxylation, the decarboxylation step contributes only slightly to rate limitation, overview Saccharomyces cerevisiae
isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH + H+ chemical mechanism on the basis of the pH dependence of kinetic parameters, dissociation constants for competitive inhibitors, and multiple-substrate deuterium/13C isotope effects suggesting a stepwise mechanism with hydride transfer preceding decarboxylation, the decarboxylation step contributes only slightly to rate limitation, overview Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ chemical mechanism, stereochemistry of hydride transfer to NAD, overview Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH + H+
-
?
isocitrate + NAD+ rapid equilibrium random catalytic mechanism, stereochemistry of hydride transfer to NAD, overview Saccharomyces cerevisiae 2-oxoglutarate + CO2 + NADH + H+
-
?
additional information 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 Saccharomyces cerevisiae ?
-
?

Synonyms

Synonyms Comment Organism
3-carboxy-2-hydroxyadipate dehydrogenase
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Saccharomyces cerevisiae
HICDH
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Saccharomyces cerevisiae
homoisocitrate dehydrogenase
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Saccharomyces cerevisiae
More HIcDH is a member of the family of pyridine nucleotide-linked beta-hydroxy acid oxidative decarboxylases Saccharomyces cerevisiae

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
5 10 pH-profile, overview Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+ stereochemistry of hydride transfer to NAD, overview Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.043
-
3-carboxypropylidenemalate pH 8.0, 25┬░C, versus homoisocitrate Saccharomyces cerevisiae