Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-D-alanine and D-alanyl-D-lactate residues
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منابع مشابه
Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-D-alanine and D-alanyl-D-lactate residues.
LY191145 is an N-alkylated glycopeptide antibiotic (the p-chlorobenzyl derivative of LY264826) with activity against vancomycin-susceptible and -resistant bacteria. Similar to vancomycin, LY191145 inhibited polymerization of peptidoglycan when muramyl pentapeptide served as a substrate but not when muramyl tetrapeptide was used, signifying a substrate-dependent mechanism of inhibition. Examinat...
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Antibiotic A3 5512B1.2) is a member of the glycopeptide family of antibiotics; complete structures have been reported for two members of this group, vancomycin3' and ristocetin A4' a) . Both vancomycin and ristocetin have been shown to form complexes with mucopeptides containing the terminal dipeptide D-alanyl-D-alaninee) ; this interaction within the bacterial cell inhibits crosslinking of the...
متن کاملKinetic evidence for the formation of D-alanyl phosphate in the mechanism of D-alanyl-D-alanine ligase.
The steady state kinetic mechanism, molecular isotope exchange and the positional isotope exchange (PIX) reactions of D-alanyl-D-alanine ligase from Salmonella typhimurium have been studied. The kinetic mechanism has been determined to be ordered Ter-Ter from initial velocity and product inhibition experiments. The first substrate to bind is ATP followed by the addition of 2 mol of D-alanine. P...
متن کاملModifications of the acyl-D-alanyl-D-alanine terminus affecting complex-formation with vancomycin.
Vancomycin forms complexes with peptides terminating in d-alanyl-d-alanine that are analogous to the biosynthetic precursors of bacterial mucopeptides. The specificity of complex-formation has been studied by means of many synthetic peptides, prepared by both solid-phase and conventional methods. The following conclusions can be drawn: (a) three amide linkages are required to form a stable comp...
متن کاملKinetic study of interaction between BRL 42715, beta-lactamases, and D-alanyl-D-alanine peptidases.
A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4) is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn(2+)-containing enzymes, with very different kcat value...
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 1997
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.41.1.66