Chromogenic depsipeptide substrates for beta-lactamases and penicillin-sensitive DD-peptidases.
Various ester and thioester derivatives of hippuric acid have been prepared which were substrates of both beta-lactamases and DD-peptidases. The thioesters were more rapidly hydrolysed by nearly all the enzymes. Surprisingly, the enzymes acted rather efficiently on substrates which did not contain any chiral centre.
Laboratoire d'Enzymologie, Université de Liĕge, Sart Tilman, Belgium.
M
M
Adam
C
C
Damblon
B
B
Plaitin
L
L
Christiaens
J M
JM
Frère
D000595:Amino Acid Sequence; D002863:Chromogenic Compounds / Q000378:metabolism*; D004952:Esters; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D015394:Molecular Structure; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism*; D010406:Penicillins / Q000494:pharmacology*; D011402:Pronase / Q000378:metabolism; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000378:metabolism*
D002863:Chromogenic Compounds; D004952:Esters; D009842:Oligopeptides; D010406:Penicillins; D002267:Muramoylpentapeptide Carboxypeptidase; D011402:Pronase; D001618:beta-Lactamases