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Literature summary for 1.1.1.87 extracted from

  • Rowley, B.; Tucci, A.F.
    Homoisocitric dehydrogenase from yeast (1970), Arch. Biochem. Biophys., 141, 499-510.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-oxoadipate required for reductive carboxylation Saccharomyces cerevisiae
NaHCO3-CO2 required for reductive carboxylation Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
homoisocitrate 1.2 mM Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
homoisocitrate value below Saccharomyces cerevisiae
0.065
-
NADH
-
Saccharomyces cerevisiae
0.33
-
NAD+
-
Saccharomyces cerevisiae
1.5
-
alpha-ketoadipate
-
Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required for optimal activity Saccharomyces cerevisiae
Mg2+ stimulation of oxidative decarboxylation, required for reductive carboxylation Saccharomyces cerevisiae
Mn2+ stimulation of oxidative decarboxylation Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-hydroxy-1,2,4-butanetricarboxylate + NAD+ Saccharomyces cerevisiae
-
2-oxoadipate + CO2 + NADH
-
r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.8
-
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-hydroxy-1,2,4-butanetricarboxylate + NAD+
-
Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH
-
r
1-hydroxy-1,2,4-butanetricarboxylate + NAD+ i.e. homoisocitrate Saccharomyces cerevisiae 2-oxoadipate + CO2 + NADH
-
r
additional information catalyzes keto-enol tautomerization of tritiated alpha-ketoadipate, not: ethanol, isocitrate, malate, glutamate Saccharomyces cerevisiae ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
reductive carboxylation Saccharomyces cerevisiae
8.3 8.8 oxidative decarboxylation Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
6.1 7.7 pH 6.1: about 60% of activity maximum, pH 7.7: about 50% of activity maximum, reductive carboxylation Saccharomyces cerevisiae
7.4 9.3 pH 7.4: about 50% of activity maximum, pH 9.3: about 90% of activity maximum, oxidative decarboxylation Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae