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.
Adam
M
M
Laboratoire d'Enzymologie, Université de Liĕge, Sart Tilman, Belgium.
Damblon
C
C
Plaitin
B
B
Christiaens
L
L
Frère
J M
JM
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