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, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5 degrees C.
Torres-Bacete
Jesús
J
Departamento de Bioquímica y Biología Molecular I, Facultad de Biología, Universidad Complutense, C/ José Antonio Nováis 2, 28040 Madrid, Spain.
Hormigo
Daniel
D
Stuart
Maribel
M
Arroyo
Miguel
M
Torres
Pedro
P
Castillón
María P
MP
Acebal
Carmen
C
García
José L
JL
de la Mata
Isabel
I
D000192:Actinomycetales / Q000201:enzymology* / Q000235:genetics; D000581:Amidohydrolases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002942:Circular Dichroism; D004795:Enzyme Stability; D015394:Molecular Structure; D010399:Penicillin Amidase / Q000235:genetics / Q000378:metabolism*; D010404:Penicillin V / Q000737:chemistry / Q000378:metabolism; D010456:Peptides, Cyclic / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D001426:Bacterial Proteins; D010456:Peptides, Cyclic; D011994:Recombinant Proteins; C011634:aculeacin A; D000581:Amidohydrolases; C060671:aculeacin A acylase; D010399:Penicillin Amidase; D010404:Penicillin V