Protein Variants | Comment | Organism |
---|---|---|
D274A | site-directed mutagenesis, the mutant shows 5695fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour | Homo sapiens |
H206A | site-directed mutagenesis, dimerization domain mutant, the mutant shows 560fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour | Homo sapiens |
H206K | site-directed mutagenesis, dimerization domain mutant, the mutant shows 348fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour | Homo sapiens |
H206N | site-directed mutagenesis, dimerization domain mutant, the mutant shows 11837fold reduced activity compared to the wild-type enzyme | Homo sapiens |
N263D | site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme | Homo sapiens |
N263S | site-directed mutagenesis, dimerization domain mutant, the mutant shows 152fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour | Homo sapiens |
R276A | site-directed mutagenesis, dimerization domain mutant, the mutant shows 8995fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour | Homo sapiens |
R276N | site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme | Homo sapiens |
R276Q | site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics of wild-type and mutant enzymes, kinetics of mutants N263D, R276N, and R276Q are not measurable | Homo sapiens | |
0.39 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant D274A | Homo sapiens | |
0.43 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant wild-type enzyme | Homo sapiens | |
0.54 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant H206A | Homo sapiens | |
0.58 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant H206K | Homo sapiens | |
0.78 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant N263D | Homo sapiens | |
2.02 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant H206N | Homo sapiens | |
67.4 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant R276A | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | binding site structure, H206 and E146 are involved | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate | active site structure, catalysis involves residues H206, N263, R276, and D274, the dimerization domain residues play important roles in binding and catalysis, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Nalpha-acetylmethionine + H2O | - |
Homo sapiens | acetate + L-methionine | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | dimerization domain residues play important roles in binding and catalysis, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Acy1 | - |
Homo sapiens |
aminoacylase-1 | - |
Homo sapiens |
More | the enzyme belongs to the M20 metallopeptidase family | Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of mutants N263D, R276N, and R276Q are not measurable | Homo sapiens | |
0.006 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant D274A | Homo sapiens | |
0.015 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant H206N | Homo sapiens | |
0.086 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant H206A | Homo sapiens | |
0.149 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant H206K | Homo sapiens | |
0.458 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant N263D | Homo sapiens | |
0.667 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant mutant R276A | Homo sapiens | |
38.3 | - |
Nalpha-acetylmethionine | pH 7.4, 22°C, recombinant wild-type enzyme | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |