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Literature summary for 5.4.99.1 extracted from

  • Kozlowski, P.M.; Kamachi, T.; Kumar, M.; Nakayama, T.; Yoshizawa, K.
    Theoretical analysis of the diradical nature of adenosylcobalamin cofactor-tyrosine complex in B12-dependent mutases: inspiring PCET-driven enzymatic catalysis (2010), J. Phys. Chem. B, 114, 5928-5939.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium P80077 methylaspartate mutase E chain (subunit epsilon)
-
Clostridium cochlearium P80078 methylaspartate mutase S chain (subunit sigma)
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Glm
-
Clostridium cochlearium
Glutamate mutase
-
Clostridium cochlearium

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin
-
Clostridium cochlearium