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

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, aculeac...

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Veröffentlicht in:	Applied and Environmental Microbiology 2007-08, Vol.73 (16), p.5378-5381
Hauptverfasser:	Torres-Bacete, Jesús, Hormigo, Daniel, Stuart, Maribel, Arroyo, Miguel, Torres, Pedro, Castillón, María P, Acebal, Carmen, García, José L, de la Mata, Isabel
Format:	Artikel
Sprache:	eng
Schlagworte:	Actinomycetales - enzymology Actinomycetales - genetics Actinoplanes Amidohydrolases - genetics Amidohydrolases - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Biological and medical sciences Circular Dichroism Enzyme Stability Enzymes Enzymology and Protein Engineering Fundamental and applied biological sciences. Psychology Microbiology Molecular Structure Penicillin Penicillin Amidase - genetics Penicillin Amidase - metabolism Penicillin V - chemistry Penicillin V - metabolism Peptides Peptides, Cyclic - chemistry Peptides, Cyclic - metabolism Recombinant Proteins - metabolism Streptomyces lividans Substrate Specificity Temperature
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Zusammenfassung:	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°C.
ISSN:	0099-2240 1098-5336
DOI:	10.1128/AEM.00452-07