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Literature summary extracted from

  • Zelder, O.; Beatrix, B.; Leutbecher, U.; Buckel, W.
    Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli (1994), Eur. J. Biochem., 226, 577-585.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.1 overexpression of polypeptide chains sigma and epsilon in Escherichia coli Clostridium cochlearium

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.1 2-Methyleneglutaric acid
-
 Clostridium cochlearium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.1 Glu Clostridium cochlearium first step in Glu fermentation pathway ?
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.1 purification of component E and component S Clostridium cochlearium

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 Glu first step in Glu fermentation pathway Clostridium cochlearium ?
-
 ?
5.4.99.1 L-Glu
-
 Clostridium cochlearium threo-3-Methylaspartate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.99.1 ? component E is a dimer, epsilon2, with epsilon = MW 53500, + component S is a monomer, sigma = 14800 Clostridium cochlearium

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.1 Cobalamin dependent on Clostridium cochlearium
5.4.99.1 Cobalamin component S binds coenzyme B12 Clostridium cochlearium