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Literature summary for 1.1.1.87 extracted from

  • Miyazaki, K.
    Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of beta-decarboxylating dehydrogenase (2005), Biochem. Biophys. Res. Commun., 331, 341-346.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0164
-
isocitrate pH 7.8, 70°C, recombinant enzyme Pyrococcus horikoshii
0.0183
-
homoisocitrate pH 7.8, 70°C, recombinant enzyme Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-isopropylmalate + NAD+ Pyrococcus horikoshii
-
?
-
?
homoisocitrate + NAD+ Pyrococcus horikoshii
-
?
-
?
isocitrate + NAD+ Pyrococcus horikoshii
-
?
-
?
additional information Pyrococcus horikoshii the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway ?
-
?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii A4CYJ9 gene PH1722 or hdh
-

Purification (Commentary)

Purification (Comment) Organism
recombinnat His-tagged enzyme from Escherichia coli by metal affinity chromatography Pyrococcus horikoshii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-isopropylmalate + NAD+
-
Pyrococcus horikoshii ?
-
?
homoisocitrate + NAD+
-
Pyrococcus horikoshii ?
-
?
isocitrate + NAD+
-
Pyrococcus horikoshii ?
-
?
additional information the enzyme is trifunctional performing the activities of 3-isopropylmalate, isocitrate, and homoisocitrate dehydrogenase in one pathway Pyrococcus horikoshii ?
-
?

Synonyms

Synonyms Comment Organism
HICDH
-
Pyrococcus horikoshii
isocitrate-homoisocitrate dehydrogenase
-
Pyrococcus horikoshii
protein PH1722
-
Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
assay at Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.7
-
homoisocitrate pH 7.8, 70°C, recombinant enzyme Pyrococcus horikoshii
14.8
-
isocitrate pH 7.8, 70°C, recombinant enzyme Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Pyrococcus horikoshii