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Literature summary for 5.4.99.1 extracted from

  • Holloway, D.E.; Chen, H.P.; Marsh, E.N.G.
    Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase (1996), J. Biol. Chem., 271, 29121-29125.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C15A Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive Clostridium tetanomorphum
C15N Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive Clostridium tetanomorphum
C15S Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive Clostridium tetanomorphum

Inhibitors

Inhibitors Comment Organism Structure
iodoacetate specifically alkylates Cys15 in enzyme component S with concomitant irreversible loss of enzyme activity Clostridium tetanomorphum

Organism

Organism UniProt Comment Textmining
Clostridium tetanomorphum
-
-
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
Cobalamin dependent on Clostridium tetanomorphum
Cobalamin coenzyme binding and catalysis is very sensitive to mutations at position 15 Clostridium tetanomorphum