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Literature summary for 5.4.99.1 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)

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

Inhibitors

Inhibitors Comment Organism Structure
2-Methyleneglutaric acid
-
Clostridium cochlearium

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glu first step in Glu fermentation pathway Clostridium cochlearium ?
-
?
L-Glu
-
Clostridium cochlearium threo-3-Methylaspartate
-
?

Subunits

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

Cofactor

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