A Genetic Approach to the Study of CAD
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Marcia Steinberg', 'PO_EMAI': None, 'PO_PHON': None}
The first three enzymes of de novo pyrimidine biosynthesis                      are the same from bacteria to humans.  Yet the structure,                       organization, and regulation of the enzymes and their                           respective genes have changed considerably.  In mammals the                     enzymes, carbamyl phosphate synthetase II, aspartate                            transcarbamylase, and dihyroorotase, are found together in a                    single translation product called CAD.  Most studies have                       been limited to biochemical analysis of purified protein or                     proteolytic fragments derived from it.  However, we have                        developed a strategy for expressing individual enzymatic                        domains of hamster CAD in E. coli.  This now allows us to                       introduce genetic changes into the DNA sequence and observe                     the effects on enzyme structure and function.  For this work                    we will exploit this strategy for analyzing each enzyme of                      the CAD protein and for comparing the CAD domains to their                      monofunctional counterparts in bacteria.  Through a series of                                                                                                   experiments involving molecular biological, genetic, and                        biochemical methods, we hope to learn much about the                            structure, function, and evolution of a multifunctional                         protein that plays a key role in an important biosynthetic                      pathway.
{'FirstName': 'Jeffrey', 'LastName': 'Davidson', 'PI_MID_INIT': 'N', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Jeffrey N Davidson', 'EmailAddress': 'jndavid@pop.uky.edu', 'NSF_ID': '000098154', 'StartDate': '07/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Kentucky Research Foundation', 'CityName': 'LEXINGTON', 'ZipCode': '405260001', 'PhoneNumber': '8592579420', 'StreetAddress': '500 S LIMESTONE', 'StreetAddress2': '109 KINKEAD HALL', 'CountryName': 'United States', 'StateName': 'Kentucky', 'StateCode': 'KY', 'CONGRESSDISTRICT': '06', 'CONGRESS_DISTRICT_ORG': 'KY06', 'ORG_UEI_NUM': 'H1HYA8Z1NTM5', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF KENTUCKY RESEARCH FOUNDATION, THE', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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