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• W2108481608 abstract "An N-carbamoyl-beta-alanine amidohydrolase of industrial interest from Agrobacterium tumefaciens C58 (beta car(At)) has been characterized. Beta car(At) is most active at 30 degrees C and pH 8.0 with N-carbamoyl-beta-alanine as a substrate. The purified enzyme is completely inactivated by the metal-chelating agent 8-hydroxyquinoline-5-sulfonic acid (HQSA), and activity is restored by the addition of divalent metal ions, such as Mn(2+), Ni(2+), and Co(2+). The native enzyme is a homodimer with a molecular mass of 90 kDa from pH 5.5 to 9.0. The enzyme has a broad substrate spectrum and hydrolyzes nonsubstituted N-carbamoyl-alpha-, -beta-, -gamma-, and -delta-amino acids, with the greatest catalytic efficiency for N-carbamoyl-beta-alanine. Beta car(At) also recognizes substrate analogues substituted with sulfonic and phosphonic acid groups to produce the beta-amino acids taurine and ciliatine, respectively. Beta car(At) is able to produce monosubstituted beta(2)- and beta(3)-amino acids, showing better catalytic efficiency (k(cat)/K(m)) for the production of the former. For both types of monosubstituted substrates, the enzyme hydrolyzes N-carbamoyl-beta-amino acids with a short aliphatic side chain better than those with aromatic rings. These properties make beta car(At) an outstanding candidate for application in the biotechnology industry." @default.
• W2108481608 created "2016-06-24" @default.
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• W2108481608 date "2009-01-15" @default.
• W2108481608 modified "2023-10-18" @default.
• W2108481608 title "Potential Application of<i>N</i>-Carbamoyl-β-Alanine Amidohydrolase from<i>Agrobacterium tumefaciens</i>C58 for β-Amino Acid Production" @default.
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• W2108481608 doi "https://doi.org/10.1128/aem.01128-08" @default.
• W2108481608 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2620706" @default.
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