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Literature summary extracted from

  • Stokke, R.; Madern, D.; Fedoy, A.; Karlsen, S.; Birkeland, N.; Steen, I.H.
    Biochemical characterization of isocitrate dehydrogenase from Methylococcus capsulatus reveals a unique NAD+-dependent homotetrameric enzyme (2007), Arch. Microbiol., 187, 361-370.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.41 cloned and overexpressed in Escherichia coli Methylococcus capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.41 0.0517
-
isocitrate
-
Methylococcus capsulatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.41 36340
-
4 * 36340, the clasp-like domain of McIDH is a likely site for tetramerization, calculated from sequence Methylococcus capsulatus
1.1.1.41 145000
-
gel filtration Methylococcus capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.41 Methylococcus capsulatus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.41
-
Methylococcus capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.41 isocitrate + NAD+ the enzyme is NAD+-dependent Methylococcus capsulatus 2-oxoglutarate + CO2 + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.41 tetramer 4 * 36340, the clasp-like domain of McIDH is a likely site for tetramerization, calculated from sequence Methylococcus capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.41 McIDH
-
Methylococcus capsulatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.41 55 60
-
Methylococcus capsulatus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.41 70
-
apparent midpoint melting temperature Methylococcus capsulatus