Crystallization (Comment) | Organism |
---|---|
crystal structure of the inactive H220A mutant displays that the endogenous Zn2+ shifts to alpha3 subsite coordinated by His67, His69, Cys96 and Asp366 | Alcaligenes faecalis |
Protein Variants | Comment | Organism |
---|---|---|
C96D | inactive mutant enzymes | Alcaligenes faecalis |
D366A | inactive mutant enzymes | Alcaligenes faecalis |
H220A | inactive mutant enzymes | Alcaligenes faecalis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cd2+ | noncompetitive, binds at the alpha1 subsite ligated by His67, His69 and Asp366 | Alcaligenes faecalis | |
Cu2+ | noncompetitive, binds at the alpha2 subsite chelated by His67, His69 and Cys96 | Alcaligenes faecalis | |
additional information | no inhibition by Ni2+, Co2+, Mg2+, Mn2+ and Ca2+ | Alcaligenes faecalis | |
Zn2+ | noncompetitive, binds at the alpha1 subsite ligated by His67, His69 and Asp366 | Alcaligenes faecalis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.59 | - |
N-Acetyl-D-Met | wild-type enzyme | Alcaligenes faecalis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | catalytically essential Zn2+ is tightly bound at the beta site with coordination by Cys96, His220 and His250 | Alcaligenes faecalis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcaligenes faecalis | Q9AGH8 | - |
- |
Alcaligenes faecalis DA1 | Q9AGH8 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-Acetyl-D-Met + H2O | - |
Alcaligenes faecalis | acetate + D-Met | - |
? | |
N-Acetyl-D-Met + H2O | - |
Alcaligenes faecalis DA1 | acetate + D-Met | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
438 | - |
N-Acetyl-D-Met | wild-type enzyme | Alcaligenes faecalis |