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Literature summary 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

EC Number Organism UniProt Comment Textmining
5.4.99.1 Clostridium cochlearium
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.99.1 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
a
5.4.99.1 L-threo-3-methylaspartate = L-glutamate the 4-glutamyl radical is an intermediate in the carbon skeleton rearrangement catalyzed the enzyme Clostridium cochlearium
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.1 Cobalamin dependent on Clostridium cochlearium