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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actinomycetales / enzymology*
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Actinomycetales / genetics
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Amidohydrolases / genetics
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Amidohydrolases / metabolism*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Circular Dichroism
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Enzyme Stability
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Molecular Structure
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Penicillin Amidase / genetics
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Penicillin Amidase / metabolism*
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Penicillin V / chemistry
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Penicillin V / metabolism
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / metabolism
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Recombinant Proteins / metabolism
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Substrate Specificity
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Temperature
Substances
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Bacterial Proteins
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Peptides, Cyclic
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Recombinant Proteins
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aculeacin A
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Amidohydrolases
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aculeacin A acylase
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Penicillin Amidase
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Penicillin V