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Literature summary extracted from

  • Lin, Y.; West, A.H.; Cook, P.F.
    Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae (2009), Biochemistry, 48, 7305-7312.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.87 K206M site-directed mutagenesis, the active site mutant shows about 2400fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly Saccharomyces cerevisiae
1.1.1.87 Y150F site-directed mutagenesis, the active site mutant shows about 680fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.87 additional information
-
 additional information mutant enzymes kinetic analysis and pH-dependencies, overview Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.87 K+ dependent on Saccharomyces cerevisiae
1.1.1.87 Mg2+ dependent on Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.87 (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ Saccharomyces cerevisiae
-
 2-oxoadipate + NADH + H+ + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.87 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.87 HIc dehydrogenase
-
 Saccharomyces cerevisiae
1.1.1.87 HICDH
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.87 25
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.87 additional information
-
 mutant enzymes kinetics and pH-dependencies, overview Saccharomyces cerevisiae
1.1.1.87 7.5
-
 assay at Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.87 6.2 9.5
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.87 NAD+
-
 Saccharomyces cerevisiae