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Literature summary extracted from

  • Michel, C.; Hartrampf, G.; Buckel, W.
    Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri (1989), Eur. J. Biochem., 184, 103-107.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.99.4 4
-
2-Methyleneglutarate
-
Eubacterium barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.99.4 70000
-
4 * 70000, SDS-PAGE Eubacterium barkeri
5.4.99.4 290000
-
gel filtration Eubacterium barkeri

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.4 Eubacterium barkeri
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.4
-
Eubacterium barkeri

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.4.99.4 additional information
-
continuous spectrophotometric assay Eubacterium barkeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.4 2-Methyleneglutarate
-
Eubacterium barkeri 2-Methylene-3-methylsuccinate
-
?

Subunits

EC Number Subunits Comment Organism
5.4.99.4 tetramer 4 * 70000, SDS-PAGE Eubacterium barkeri

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.4 cobamide dependent on Eubacterium barkeri