Characterization of mevalonate diphosphate decarboxylase and isopentenyl diphosphate isomerase in Enterococcus faecalis
Abstract
Emerging antibiotic resistant strains of bacteria such as Methicillin Resistant Staphylococcus aureus (MRSA) and Vancomycin Resistant Enterococcus (VRE) are common causes of nosocomial infections. Recent data indicate deaths from hospital based infections have surpassed those from HIV/AIDS in the United States and are a health concern worldwide amid a decline in new antibiotic development. Isopentenyl Pyrophosphate (IPP) is the 5-carbon precursor of over 20,000 compounds in living systems including cholesterol, steroids, carotenoids, and lipids. Two pathways have been identified for the synthesis of IPP, the mevalonate pathway and the glyceraldehyde-3-phosphate pathway. Gene knockout experiments show enzymes of the mevalonate pathway to be essential in many gram-positive bacteria including E. faecalis, thus making them a target for a novel antibiotic. Mevalonate diphosphate decarboxylase (MDD) and Isopentenyl diphosphate isomerase (IDI) represent the next enzymes of the E. faecalis mevalonate pathway to be characterized. MDD and IDI cloning, expression, purification, and crystallization trials are herein reported.
Degree
M.S.
Advisors
Stauffacher, Purdue University.
Subject Area
Molecular biology|Microbiology|Biochemistry
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