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Literature summary 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

Application

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

Cloned(Commentary)

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

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.14 Sus scrofa P37111
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.14 kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.5.1.14 More structural homology modeling, overview Sus scrofa

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.14 25
-
 assay at Sus scrofa

pH Optimum

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

pH Range

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