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Literature summary for 5.4.99.1 extracted from

  • Bothe, H.; Darley, D.J.; Albracht, S.P.; Gerfen, G.J.; Golding, B.T.; Buckel, W.
    Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium (1998), Biochemistry, 37, 4105-4113.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-threo-3-methylaspartate = L-glutamate the reaction is initiated through hydrogen atom abstraction from C-4 of Glu by 5'-deoxyadenosyl radical which is derived by homolysis of the Co-C sigma-bond of coenzyme B12 Clostridium cochlearium
L-threo-3-methylaspartate = L-glutamate the 4-glutamyl radical is an intermediate in the carbon skeleton rearrangement catalyzed the enzyme Clostridium cochlearium

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Glu
-
Clostridium cochlearium threo-3-Methylaspartate
-
?

Cofactor

Cofactor Comment Organism Structure
Cobalamin dependent on Clostridium cochlearium