KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | analysis of limiting rate constants of reaction with benzylamine and deuterated benzylamine at different pH values | Alcaligenes faecalis | |
6.7 | - |
benzylamine | pH 7.5, 25°C, native enzyme | Alcaligenes faecalis | |
9.9 | - |
benzylamine | pH 7.5, 25°C, recombinant enzyme | Alcaligenes faecalis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcaligenes faecalis | - |
expression in Paracoccus denitrificans | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme, expression in Paracoccus denitrificans | Alcaligenes faecalis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin | breakage of the substrate C-H bond occurs via quantum mechanical tunneling. In steady-state reactions with benzylamine, breakage of C-H bond is only partially rate-limiting | Alcaligenes faecalis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
30.8 | - |
pH 7.5, 25°C | Alcaligenes faecalis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzylamine + H2O + 2,6-dichlorophenol | analysis of limiting rate constants | Alcaligenes faecalis | ? + NH3 + reduced 2,6-dichlorophenol indophenol | - |
? | |
phenazine ethosulfate + H2O + 2,6-dichlorophenol indophenol | - |
Alcaligenes faecalis | ? + NH3 + reduced 2,6-dichlorophenol indophenol | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.02 | - |
benzylamine | pH 7.5, 25°C, recombinant enzyme | Alcaligenes faecalis | |
1.14 | - |
benzylamine | pH 7.5, 25°C, native enzyme | Alcaligenes faecalis |