Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.99.4 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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Eubacterium barkeri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Eubacterium barkeri

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
cobamide dependent on Eubacterium barkeri