The Energetics of Enzyme Catalysis
{'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 work is aimed at a deeper understanding of the nature of                   enzyme catalysis.  Two groups of enzymes will be studied.                       First, the mechanism of amino acid racemases will be                            investigated, with particular focus on glutamate racemase and                   diaminopimelate empimerase.  Each of these enzymes catalyzes                    the racemization of an  x-amino acid center without the need                    for or involvement of pyridoxal phosphate.  The enzymes will be                 isolated and characterized, and the energetics of their                         reactions will be explored by the use of isotope exchange,                      isotope tracer, and perturbation experiments.  The second group                 of enzymes are the hydratases, and the primary goal here will                   be to determine whether the reactions proceed in a concerted or                 stepwise fashion.  The double isotope fractionation test will                   be used, and a new protocol will be evaluated that has the                      potential for extending this methodology to previously                          inappropriate systems.  Hydrations that proceed with anti                       stereochemistry will be compared with those that follow a syn                   pathway.  Together, the studies proposed will provide                           information about the intimate mechanistic details of these                     very efficient reactions.                                                                                                                                       Enzymes are formidably efficient catalysts that mediate                         specific chemical transformations at rates rarely approached by                 even the best of man-made catalytic assemblies.  If we could                    trace the development of catalytic efficiency we should be                      better able to understand the nature of enzyme catalysis as we                  find it today.  Dr. Knowles is certainly making headway with                    his incisive attack on simple systems.
{'FirstName': 'Jeremy', 'LastName': 'Knowles', 'PI_MID_INIT': 'R', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Jeremy R Knowles', 'EmailAddress': None, 'NSF_ID': '000446458', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Harvard University', 'CityName': 'CAMBRIDGE', 'ZipCode': '021385366', 'PhoneNumber': '6174955501', 'StreetAddress': '1033 MASSACHUSETTS AVE STE 3', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Massachusetts', 'StateCode': 'MA', 'CONGRESSDISTRICT': '05', 'CONGRESS_DISTRICT_ORG': 'MA05', 'ORG_UEI_NUM': 'LN53LCFJFL45', 'ORG_LGL_BUS_NAME': 'PRESIDENT AND FELLOWS OF HARVARD COLLEGE', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1166', 'Text': 'MOLECULAR BIOCHEMISTRY'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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