Decarboxylase Structure-Function Relationships
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
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A structural feature common to apoproteins of all pyridoxal                     5'-phosphate (PLP) dependent carboxylases is an active site                     lysine which forms a Schiff base between the epsilon amino                      group and the aldehyde moiety of the cofactor.  Dialkyl                         glycine decarboxylase (DGD) from Pseudomonas cepacia is                         probably such an enzyme.  It can catalyze both                                  decarboxylation and transamination reactions.  Previous work                    with this enzyme suggests that the proton transfer is                           unusual. DGD catalyzes proton transfer to the 4' carbon of                      the cofactor instead of the alpha carbon of the amino                           acid.  A reasonable hypothesis is that DGD is structurally                      similar to other decarboxylases but differs from them by                        inverting the basicities of histidine and lysine.  This                         change would place the solvent proton preferentially on                         lysine which is closer to the cofactor 4' carbon.  In order                     to test the validity of this model, mutants will be                             constucted with alanine substituting for the lysine at the                      active site.  If the experimental outcome confirms this                         hypothesis, it will tell us a good deal about the electric                      field strengths at the active site and how such local fields                    affect the free energy contents of enzyme-substrates                            complexes and transition states.  Dr. Keller is conversant                      with the enzyme and has been well trained.  The project would                   have a fovarable impact on the quality of undergraduate                         education at the host institution.
{'FirstName': 'John', 'LastName': 'Keller', 'PI_MID_INIT': 'W', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'John W Keller', 'EmailAddress': 'jwkeller@alaska.edu', 'NSF_ID': '000151850', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
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[{'Code': '114400', 'Text': 'Molecular Biophysics'}, {'Code': '912000', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}, {'Code': '914500', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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