Application | Comment | Organism |
---|---|---|
synthesis | pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the enzyme acts as chiral catalyst | Sus scrofa |
Cloned (Comment) | Organism |
---|---|
expression of pAcy1 in Escherichia coli strain BL21 (DE3) | Sus scrofa |
Protein Variants | Comment | Organism |
---|---|---|
D346A | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis, by 4000fold, at pH 7.5, the pH optimum with substrate 3-(2-furyl)acryloyl-L-methionine is altered compared to the wild-type enzyme | Sus scrofa |
D346E | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5 | Sus scrofa |
D346N | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5 | Sus scrofa |
D346Q | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5, the pH optimum with substrate 3-(2-furyl)acryloyl-L-methionine is altered compared to the wild-type enzyme | Sus scrofa |
E146A | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5 | Sus scrofa |
E146D | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5 | Sus scrofa |
E146N | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5 | Sus scrofa |
E146Q | site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5 | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Sus scrofa | pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the catalytic base is E146. pAcy1 from pig kidney displays a marked preference for short-chain acyl moieties and non-branched aliphatic L-amino acids. Modeling of pAcy1 catalyzed N-acylation, overview | ? | - |
? | |
N-acetyl-L-methionine + H2O | Sus scrofa | - |
acetate + L-methionine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | P37111 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | - |
Sus scrofa | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2.9 | - |
recombinant wild-type enzyme, substrate L-methionine, synthesis reaction, pH 6.0, 25°C | Sus scrofa |
77 | - |
recombinant wild-type enzyme, substrate N-acetyl-L-methionine, hydrolytic reaction, pH 6.0, 25°C | Sus scrofa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-(2-furyl)acryloyl-L-methionine + H2O | - |
Sus scrofa | 3-(2-furyl)acrylate + L-methionine | - |
? | |
additional information | pAcy1 catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids, the catalytic base is E146. pAcy1 from pig kidney displays a marked preference for short-chain acyl moieties and non-branched aliphatic L-amino acids. Modeling of pAcy1 catalyzed N-acylation, overview | Sus scrofa | ? | - |
? | |
N-acetyl-L-methionine + H2O | - |
Sus scrofa | acetate + L-methionine | - |
? | |
N-acetyl-L-methionine + H2O | - |
Sus scrofa | acetate + L-methionine | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | structural homology modeling, overview | Sus scrofa |
Synonyms | Comment | Organism |
---|---|---|
aminoacylase 1 | - |
Sus scrofa |
N-acyl-L-amino acid amidohydrolase | - |
Sus scrofa |
pAcy1 | - |
Sus scrofa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Sus scrofa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
synthesis of N-acetyl-L-methionine | Sus scrofa |
7.2 | - |
hydrolysis of 3-(2-furyl)acryloyl-L-methionine | Sus scrofa |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.5 | 7.2 | activity range, substrate N-acetyl-L-methionine | Sus scrofa |