Mechanism of Histidinol Dehydrogenase
{'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 renewal proposal will continue ongoing studies on the                      mechanism of Salmonella histidinol dehydrogenase (HDH), a 4-                    electron NAD-linked enzyme.  The focus is on the use of                         primary isotope effects to obtain rates for the two reaction                    steps, the chemistry of the steps, and the pK values and                        nature of the enzyme residues involved.  A high priority is                     assigned to completing the stereochemistry of the                               dehydrogenation reactions.  Although important binding                          interactions of histidinol with HDH at the imidozole ring and                   amino regions have been identified, the relative positions of                   these two groups in space are not known.  Rigid histamine                       receptor agonists will be used to determine this topography.                    In order to identify the active site residues involved in                       binding or catalysis, site directed modification and                            mutagenesis will be used.  Logical modifiers are being                          synthesized.                                                                                                                                                    In addition to the inherent enzyme mechanistic interest in                      HDH, the system is of broad importance in biology.  The                         enzyme is coded for by the hisD gene of the Salmonella                          histidine operon, a particularly well studied genetic system.                   The known mutants in the system form the basis for the well                     known Ames test.
{'FirstName': 'Charles', 'LastName': 'Grubmeyer', 'PI_MID_INIT': 'T', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Charles T Grubmeyer', 'EmailAddress': 'ctg@temple.edu', 'PI_PHON': None, 'NSF_ID': '000089283', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
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[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}]
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