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Literature summary for 3.5.1.14 extracted from

  • Wardenga, R.; Lindner, H.A.; Hollmann, F.; Thum, O.; Bornscheuer, U.
    Increasing the synthesis/hydrolysis ratio of aminoacylase 1 by site-directed mutagenesis (2010), Biochimie, 92, 102-109.
    View publication on PubMed
Search for more literature for 3.5.1.14

Application

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(Commentary)

Cloned (Comment) Organism
expression of pAcy1 in Escherichia coli strain BL21 (DE3) Sus scrofa

Protein Variants

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Sus scrofa P37111
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
More structural homology modeling, overview Sus scrofa

Synonyms

Synonyms Comment Organism
aminoacylase 1
-
 Sus scrofa
N-acyl-L-amino acid amidohydrolase
-
 Sus scrofa
pAcy1
-
 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Sus scrofa

pH Optimum

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 Range

pH Minimum pH Maximum Comment Organism
4.5 7.2 activity range, substrate N-acetyl-L-methionine Sus scrofa