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Applied and Environmental Microbiology
Article . 2007 . Peer-reviewed
License: ASM Journals Non-Commercial TDM
Data sources: Crossref
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Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis

Authors: García, José Luis; Hormigo, Daniel; Stuart, Maribel; Arroyo, Miguel; Torres, Pedro; Torres-Bacete, Jesús; Castillón, María Pilar; +2 Authors

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

Abstract

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°C.

Keywords

Molecular Structure, Circular Dichroism, Temperature, Peptides, Cyclic, Recombinant Proteins, Amidohydrolases, Substrate Specificity, Bacterial Proteins, Actinomycetales, Enzyme Stability, Penicillin V, Penicillin Amidase

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selected citations
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This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
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