Disease relevance of Quinacillin

• The inactivation of RTEM-2 beta-lactamase and of Bacillus cereus beta-lactamase I is accelerated in the presence of A type substrates such as dicloxacillin, quinacillin, and cefoxitin, which are thought to expand or loosen the conformation of these enzymes [1].
• The active site of penicillinase from Staphylococcus aureus PC1. Isolation of a specific covalent complex with the substrate quinacillin [2].

High impact information on Quinacillin

• Reversible deactivation of beta-lactamase by quinacillin. Extent of the conformational change in the isolated transitory complex [3].
• 1. The penicillinase-catalysed hydrolysis of quinacillin was quenched by addition of 5 m-guanidinium chloride or 1% (w/v) sodium dodecyl sulphate, and the quenched reaction mixture was dialysed exhaustively against solutions of the denaturant [2].

Chemical compound and disease context of Quinacillin

• The effect of antibody on the reversible deactivation of the beta-lactamase (penicillin amino-beta-lactamhydrolase, EC 3.5.2.6) from Staphylococcus aureus has been studied using quinacillin and cephaloridine as substrates [4].

Biological context of Quinacillin

• 5. 4. Chymotryptic hydrolysis of the product and subsequent fractionation showed that quinacillin was bound to one or possibly two peptides [2].

Associations of Quinacillin with other chemical compounds

• Continuous assays for following the hydrolysis of quinacillin and cephaloridine by optical rotation are reported [4].

References