EC Number | Application | Comment | Organism |
---|---|---|---|
3.5.1.14 | 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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.14 | expression of pAcy1 in Escherichia coli strain BL21 (DE3) | Sus scrofa |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.14 | 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 |
3.5.1.14 | 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 |
3.5.1.14 | 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 |
3.5.1.14 | 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 |
3.5.1.14 | 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 |
3.5.1.14 | 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 |
3.5.1.14 | 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 |
3.5.1.14 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.14 | 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 | ? | - |
? | |
3.5.1.14 | N-acetyl-L-methionine + H2O | Sus scrofa | - |
acetate + L-methionine | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.14 | Sus scrofa | P37111 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.5.1.14 | kidney | - |
Sus scrofa | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 2.9 | - |
recombinant wild-type enzyme, substrate L-methionine, synthesis reaction, pH 6.0, 25°C | Sus scrofa |
3.5.1.14 | 77 | - |
recombinant wild-type enzyme, substrate N-acetyl-L-methionine, hydrolytic reaction, pH 6.0, 25°C | Sus scrofa |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.14 | 3-(2-furyl)acryloyl-L-methionine + H2O | - |
Sus scrofa | 3-(2-furyl)acrylate + L-methionine | - |
? | |
3.5.1.14 | 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 | ? | - |
? | |
3.5.1.14 | N-acetyl-L-methionine + H2O | - |
Sus scrofa | acetate + L-methionine | - |
? | |
3.5.1.14 | N-acetyl-L-methionine + H2O | - |
Sus scrofa | acetate + L-methionine | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.14 | More | structural homology modeling, overview | Sus scrofa |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.14 | aminoacylase 1 | - |
Sus scrofa |
3.5.1.14 | N-acyl-L-amino acid amidohydrolase | - |
Sus scrofa |
3.5.1.14 | pAcy1 | - |
Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 25 | - |
assay at | Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 6 | - |
synthesis of N-acetyl-L-methionine | Sus scrofa |
3.5.1.14 | 7.2 | - |
hydrolysis of 3-(2-furyl)acryloyl-L-methionine | Sus scrofa |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.14 | 4.5 | 7.2 | activity range, substrate N-acetyl-L-methionine | Sus scrofa |