Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis |
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Authors: | Torres-Bacete Jesús Hormigo Daniel Stuart Maribel Arroyo Miguel Torres Pedro Castillón María P Acebal Carmen García José L de la Mata Isabel |
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Affiliation: | Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, C/ José Antonio Nováis 2, 28040 Madrid, Spain. |
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Abstract: | Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM(-1) s(-1). Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5 degrees C. |
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