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Literature summary for 5.4.99.4 extracted from

  • Zelder, O.; Buckel, W.
    On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri (1993), Biol. Chem. Hoppe-Seyler, 374, 85-90.
    View publication on PubMed
Search for more literature for 5.4.99.4

Inhibitors

Inhibitors Comment Organism Structure
Itaconate competitive Eubacterium barkeri

Organism

Organism UniProt Comment Textmining
Eubacterium barkeri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Eubacterium barkeri

Reaction

Reaction Comment Organism Reaction ID
2-Methyleneglutarate = 2-methylene-3-methylsuccinate formation of an unusual oxygen-sensitive Co(II) species during catalysis Eubacterium barkeri
a

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
cobamide the enzyme contains adenosylcobalamin and varying amounts of oxygen-stable cob(II)alamin. The content of total cobalamin is 2-4 mol/ml enzyme, the content of cob(II)alamin is 6-11% of the total cobalamin. The oxygen-stable cob(II)alamin is not involved in catalysis Eubacterium barkeri