Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Benzimidazolribofuranosyl-adenosylcobinamide | can serve as cofactor, Km-value in reaction with L-Glu, fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit: 0.0048 mM. Km-value in reaction with L-Glu, wild-type enzyme: 0.0005 mM | Clostridium tetanomorphum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit | Clostridium tetanomorphum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.2 | - |
L-Glu | reaction with benzimidazolribofuranosyl-adenosylcobinamide, wild-type enzyme and fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit | Clostridium tetanomorphum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium tetanomorphum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit | Clostridium tetanomorphum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Glu | - |
Clostridium tetanomorphum | threo-3-Methylaspartate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.65 | - |
L-Glu | reaction of L-Glu with benzimidazolribofuranosyl-adenosylcobinamide, fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit | Clostridium tetanomorphum | |
20 | - |
L-Glu | reaction of L-Glu with benzimidazolribofuranosyl-adenosylcobinamide, wild-type enzyme | Clostridium tetanomorphum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Cobalamin | dependent on | Clostridium tetanomorphum |