Catalytic and Regulatory  Properties of Hybrid ATCases Formefrom Native and Genetically Reconstructed Subunits of       Divergent Bacteria
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Eve Ida Barak', 'PO_EMAI': None, 'PO_PHON': None}
The Aspartate transcarbamoylases (ATCases) of divergent                         organisms, and in particular of enterobacteria, are                             sufficiently similar to organize in comparable tertiary                         domains and to assemble in similar quaternary aggregates.                       Nevertheless, they differ from each other by their catalytic                    properties and allosteric responses.  Various intergenic                        fusions have been carried out from bacterial cistrons and                       hamster cDNA clones and their characterization is underway.                     The sequences of catalytic and regulatory chains have been                      determined.  These will be compared in the hope that a                          sufficient number of sequence: function comparisons will                        permit deduction of critical structure/function                                 relationships.  Site specific mutagenesis will be performed                     aimed at elucidating the function of each segment of these                      catalytic and regulatory polypeptides.  Monoclonal antibodies                   will be used to compare surface structures of the enzyme from                   different species.  Collaboration with x-ray                                    crystallographers should provide definitive structural                          information of interesting mutationally altered proteins.                       This is an excellent model system for such studies and                          Dr. Wild's past work makes him uniquely qualified for what is                   proposed.
{'FirstName': 'James', 'LastName': 'Wild', 'PI_MID_INIT': 'R', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'James R Wild', 'EmailAddress': 'j-wild@tamu.edu', 'NSF_ID': '000302463', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Texas A&M University', 'CityName': 'COLLEGE STATION', 'ZipCode': '778454375', 'PhoneNumber': '9798626777', 'StreetAddress': '400 HARVEY MITCHELL PKY S STE 30', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Texas', 'StateCode': 'TX', 'CONGRESSDISTRICT': '10', 'CONGRESS_DISTRICT_ORG': 'TX10', 'ORG_UEI_NUM': 'JF6XLNB4CDJ5', 'ORG_LGL_BUS_NAME': 'TEXAS A & M UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
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