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Literature summary for 1.1.1.41 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)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methylococcus capsulatus

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
McIDH
-
Methylococcus capsulatus

Temperature Optimum [°C]

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

Temperature Stability [°C]

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