Enzymology of metallo-B-lactamases

dc.creatorGlover, Bradley P.
dc.date.available2011-02-18T19:28:44Z
dc.date.issued1996-08
dc.degree.departmentChemistryen_US
dc.description.abstractPathogenic bacteria become resistant to penidlhns and cephalosporins through acquisition of a gene encoding the enzyme p -lactamase. (Livermore, 1991) Four classes distinguish P-lactamases as either active site serine hydrolases (class A, C and D) or zinc containmg hydrolases (class B). The class C enzyme is further distmguished from the others by being membrane bound. These bacterial enzymes catalyze the hydrolysis of the p-lactam amide group of their substrates. The class A enzyme has been studied extensively with respect to its structure, hydrolysis mechanism and inhibition. Class A enzymes proceed through an acyl-enzyme intermediate involving an active site serine residue (Fisher et al., 1980). Many substrate and transition state analogs have exhibited inhibitory effects on the class A enzyme and are used medicinally as antibiotic supplements (Wainwright, 1990). Until recently, the class B P-lactamases did not demand such study as their class A counterparts. Now, more and more clinical cases of carbapenem resistant bacteria containing the class B, zinc-requiring enzyme has caused some concern (Payne, 1993). The increased occurrence of noxious gram-positive resistant bacteria has sparked a renewed investigation into p-lactamase enzymology.
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/2346/10919en_US
dc.language.isoeng
dc.publisherTexas Tech Universityen_US
dc.rights.availabilityUnrestricted.
dc.subjectMechanism of actionen_US
dc.subjectBeta lactamasesen_US
dc.subjectCephalosporinsen_US
dc.titleEnzymology of metallo-B-lactamases
dc.typeThesis
thesis.degree.departmentChemistry
thesis.degree.departmentChemistry and Biochemistry
thesis.degree.disciplineChemistry
thesis.degree.grantorTexas Tech University
thesis.degree.levelMasters
thesis.degree.nameM.S.

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