Investigation of Enzyme Catalysis: Mechanism at the Levels  of Subunit Function and the Chemical Transformation
{'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}
This project explores the relationship betweeen the catalytic                   activities and the physical, chemical, and structural                           properties of enzymes.  Four aspects of enzyme catalysis will                   be studied: (1) The nature of the weak and strong chemical                      bonding interactions which catalyze covalent transformations                    in the reacting substrate.  (2) The influence of allosteric                     effectors on the activation energies of enzyme-catalyzed                        processes.  (3) The interrelation between enzyme                                conformational change and catalysis.  (4) Metabolite transfer                   mechanistic in bienzyme complexes which catalyze sequential                     steps in a metabolic pathway.  To investigate these                             phenomena, four enzyme systems are selected for detailed                        mechanistic studies:  (1) the liver alcohol dehydrogenases                      from human and horse liver, (2) the bienzyme, PLP-requiring                     tryptophan synthase from E. coli, (3) the PLP requiring                         cystathionine gamma-synthase from E. coli, and (4) aldehyde                     dehydrogenase from sheep liver.                                                                                                                                 The project emphasizes the use of rapid kinetic techniques                      (especially rapid scanning and single wavelength stopped-flow                   UV-visible spectroscopy) to study these systems.  Other                         techniques of importance to the project include stopped-flow                    fluorescence spectroscopy 1H and 31P FT NMR, UV-visible                         microspectrophotometry of enzyme crystals and chemical                          modification of enzyme side chain residues.  These techniques                   will be used to detect and identify chemical intermediates in                   catalysis, to search for conformational changes linked to                       catalysis, and to examine the influence of allosteric                           effectors on the interconversion of chemical intermediates on                   the catalytic path.  These studies are expected to                              significantly advance our understanding of some of the least                    well understood aspects of enzyme catalysis.
{'FirstName': 'Michael', 'LastName': 'Dunn', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Michael F Dunn', 'EmailAddress': 'michael.dunn@ucr.edu', 'NSF_ID': '000416604', 'StartDate': '11/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Riverside', 'CityName': 'RIVERSIDE', 'ZipCode': '925210001', 'PhoneNumber': '9518275535', 'StreetAddress': '200 UNIVERSTY OFC BUILDING', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '39', 'CONGRESS_DISTRICT_ORG': 'CA39', 'ORG_UEI_NUM': 'MR5QC5FCAVH5', 'ORG_LGL_BUS_NAME': 'REGENTS OF THE UNIVERSITY OF CALIFORNIA AT RIVERSIDE', 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '114400', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8703697.xml'}