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Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis

AuthorsGarcía, José Luis ; Hormigo, Daniel; Stuart, Maribel; Arroyo, Miguel; Torres, Pedro; Torres-Bacete, Jesús; Castillón, María Pilar; Acebal, Carmen; Mata, Isabel de la
Issue Date22-Jun-2007
PublisherAmerican Society for Microbiology
CitationAppl Environ Microbiol. 2007 August; 73(16): 5378–5381
PMCID: 1950969
AbstractAculeacin 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°C.
DescriptionWe express our gratitude to J. A. Salas from the University of Oviedo for providing the pEM4 expression vector.
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