Newly discovered penicillin acylase activity of aculeacin A acylase from Actinoplanes utahensis.

Authors :: Torres-Bacete J
Hormigo D
Stuart M
Arroyo M
Torres P
Castillón MP
Acebal C
García JL
de la Mata I
Source :: Applied and environmental microbiology [Appl Environ Microbiol] 2007 Aug; Vol. 73 (16), pp. 5378-81. Date of Electronic Publication: 2007 Jun 22.
Publication Year :: 2007
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.

Subjects :: Actinomycetales genetics
Amidohydrolases genetics
Bacterial Proteins genetics
Circular Dichroism
Enzyme Stability
Molecular Structure
Penicillin Amidase genetics
Penicillin V chemistry
Penicillin V metabolism
Peptides, Cyclic chemistry
Peptides, Cyclic metabolism
Recombinant Proteins metabolism
Substrate Specificity
Temperature
Actinomycetales enzymology
Amidohydrolases metabolism
Bacterial Proteins metabolism
Penicillin Amidase metabolism

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