Biochemical and mutational studies of allantoinase from Bacillus licheniformis CECT 20T
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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
2014Resumen
Allantoinases (allantoin amidohydrolase, E.C. 3.5.2.5) catalyze the hydrolysis of the amide bond of allantoin to form allantoic acid, in those organisms where allantoin is not the final product of uric acid degradation. Despite their importance in the purine catabolic pathway, sequences of microbial allantoinases with proven activity are scarce, and only the enzyme from Escherichia coli (AllEco) has been studied in detail in the genomic era. In this work, we report the cloning, purification and characterization of the recombinant allantoinase from Bacillus licheniformis CECT 20T (AllBali). The enzyme was a homotetramer with an apparent Tm of 62 1 C. Optimal parameters for the enzyme activity were pH 7.5 and 50 C, showing apparent Km and kcat values of 17.7 2.7 mM and 24.4 1.5 s 1, respectively. Co2þ proved to be the most effective cofactor, inverting the enantioselectivity of AllBali when compared to
that previously reported for other allantoinases. The common ability of diffe...
Palabra/s clave
Allantoinase
TIM-barrel
Amidohydrolase