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 | Comment | Organism | Structure |
---|---|---|---|
iodoacetate | specifically alkylates Cys15 in enzyme component S with concomitant irreversible loss of enzyme activity | Clostridium tetanomorphum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium tetanomorphum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Glu | - |
Clostridium tetanomorphum | threo-3-Methylaspartate | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Cobalamin | dependent on | Clostridium tetanomorphum | |
Cobalamin | coenzyme binding and catalysis is very sensitive to mutations at position 15 | Clostridium tetanomorphum |