Mechanistic studies of Tyrosine Hydroxylase
{'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}
Tyrosine hydroxylase, an iron-containing, pterin-dependent                      monoxygenase catalyze the rate-controlling step in the                          biosynthesis of catecholamine neurotransmitters, the                            hydroxlation of tyrosine to form dihydroxyphenylalanine.  The                   pterin-dependent monooxygenases are a poorly understood group                   of enzymes.  The primary goal of this research is to understand                 the catalytic mechanism of tyrosine hydroxylase.  The DNA for                   rat PC 12 tyrosine hydroxylase has been cloned and will be                      expressed in a high efficiency baculovirus expression system in                 order to obtain enough pure material for detailed mechanistic                   studies.  The kinetic mechanism will be determined using steady                 state kinetics and isotope trapping.  Rapid reaction techniques                 will be used to measure the rates of formation of catalytic                     intermediates.  Several nonphysiological amino acids appear to                  act as substrates for tyrosine hydroxylase; these reactions                     will be studies to gain information about the identity of the                   oxygenating species.                                                                                                                                            This class of enzymes, the monooxygenases, catalyze some of the                 most difficult reactions in biochemistry.  Consequently, they                   have been the objects of a great deal of study.  The mechanism                  of phenylalanine hydroxylase has been well studied in contrast                  to tyrosine hydroxylase.  It shows a number of significant                      differences; phenylalanine does not appear to be a substrate                    for tyrosine hydroxylase although the data is not consistent;                   the redox state of the resting enzymes are different; tyrosine                  hydroxylase can use H2 02 in place of tetrahydropterins.  This                  study could also offer fundamental insights into the mechanism                  of other classes of monooxygenases since it has features in                     common with both flavoprotein hydroxylases and Fe(11)                           monooxygenases.
{'FirstName': 'Paul', 'LastName': 'Fitzpatrick', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Paul F Fitzpatrick', 'EmailAddress': 'fitzpat@tamu.edu', 'NSF_ID': '000326675', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Texas A&M Research Foundation', 'CityName': 'COLLEGE STATION', 'ZipCode': '778454375', 'PhoneNumber': '9798626777', 'StreetAddress': '400 HARVEY MITCHELL PKWY S STE 3', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Texas', 'StateCode': 'TX', 'CONGRESSDISTRICT': '10', 'CONGRESS_DISTRICT_ORG': 'TX10', 'ORG_UEI_NUM': 'EQH8NQ4AXFT7', 'ORG_LGL_BUS_NAME': 'TEXAS A & M RESEARCH FOUNDATION', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8816407.xml'}