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Literature summary extracted from

  • Yano, S.; Haruta, H.; Ikeda, T.; Kikuchi, T.; Murakami, M.; Moriguchi, M.; Wakayama, M.
    Engineering the substrate specificity of Alcaligenes D-aminoacylase useful for the production of D-amino acids by optical resolution (2011), J. Chromatogr. B, 879, 3247-3252 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.81 biotechnology D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 is used for the biotechnological production of D-amino acid from the racemic mixture of N-acyl-DL-amino acids Achromobacter xylosoxidans
3.5.1.81 synthesis D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 is used for the biotechnological production of D-amino acid from the racemic mixture of N-acyl-DL-amino acids Achromobacter xylosoxidans

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.81 F191W site-directed mutagenesis, the catalytic efficiency of the mutant toward N-acetyl-D-Trp and N-acetyl-D-Ala is enhanced by 15.6 and 1.5folds, respectively, compared to the wild-type enzyme, with unaltered other properties, e.g. pH and temperature dependence Achromobacter xylosoxidans
3.5.1.81 L298A site-directed mutagenesis, the catalytic efficiency of the mutant toward N-acetyl-D-Trp is enhanced by 4.4folds compared to the wild-type enzyme, with unaltered other properties, e.g. pH and temperature dependence Achromobacter xylosoxidans
3.5.1.81 additional information construction of mutant AxD-NAases with substrate specificities different from those of wild-type enzyme. The substrate recognition site of the AxD-NAase is rationally manipulated based on computational structural analysis and comparison of its primary structure with other D-aminoacylases with distinct substrate specificities. Mutations of amino acid residues, Phe191, Leu298, Tyr344, and Met346, which interact with the side chain of the substrate, induce marked changes in activities toward each substrate Achromobacter xylosoxidans

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.81 Achromobacter xylosoxidans P72349
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-
3.5.1.81 Achromobacter xylosoxidans A-6 P72349
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-

Synonyms

EC Number Synonyms Comment Organism
3.5.1.81 AxD-NAase
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 Achromobacter xylosoxidans
3.5.1.81 D-Aminoacylase
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 Achromobacter xylosoxidans
3.5.1.81 dan
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 Achromobacter xylosoxidans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.81 7 10 the immobilized partially purified enzyme is most stable at pH 8.5 with over 50% stability at pH 7.0-10.0 and above Achromobacter xylosoxidans

General Information

EC Number General Information Comment Organism
3.5.1.81 additional information amino acid residues Phe191, Leu298, Tyr344, and Met346 interact with the side chain of the substrate Achromobacter xylosoxidans