Activity of penicillin-acylase-producing bacteria against alpha-aminobenzylpenicillins.
A method has been developed for the chemical analysis of individual alpha-aminobenzylpenicillin derivatives. This analytical procedure may conveniently be used to determine whether microorganisms possess penicillin acylases which show considerable activity against alpha-aminobenzylpenicillin derivatives. The method is not sufficiently sensitive to determine low levels of enzyme activity. Organisms known to produce penicillin acylases which are active against benzyl- or phenoxymethylpenicillin showed variable responses to alpha-aminobenzylpenicillin substrates. A significant difference in activity profile was noted between the intracellular enzyme of Escherichia coli and the extracellular enzyme of Bacillus megaterium.
D000581:Amidohydrolases / Q000378:metabolism*; D000667:Ampicillin / Q000378:metabolism; D001205:Ascorbic Acid / Q000378:metabolism; D001410:Bacillus megaterium / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D010399:Penicillin Amidase / Q000378:metabolism*; D010406:Penicillins / Q000378:metabolism*; D013045:Species Specificity; D013379:Substrate Specificity
D001426:Bacterial Proteins; D010406:Penicillins; D000667:Ampicillin; D000581:Amidohydrolases; D010399:Penicillin Amidase; D001205:Ascorbic Acid; C100115:hetacillin