Potential Application of N-Carbamoyl- -Alanine Amidohydrolase from Agrobacterium tumefaciens C58 for -Amino Acid Production
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Martínez Gómez, Ana Isabel![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
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Fecha
2009Resumen
An N-carbamoyl- -alanine amidohydrolase of industrial interest from Agrobacterium tumefaciens C58 ( carAt) has been characterized. carAt is most active at 30°C and pH 8.0 with N-carbamoyl- -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 Mn2 , Ni2 , and Co2 . 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- -, - -, - -, and - -amino acids, with
the greatest catalytic efficiency for N-carbamoyl- -alanine. carAt also recognizes substrate analogues substituted with sulfonic and phosphonic acid groups to produce the -amino acids taurine and ciliatine, respectively.
carAt is able to produce monosubstituted 2- and 3-amino acids, showing better catalytic efficiency (kcat/Km) for the production of the ...
Palabra/s clave
N-Carbamoyl- -Alanine Amidohydrolase
Agrobacterium tumefaciens
-Amino Acid Production