STRUCTURE OF PROLIDASE, A PROLINE-SPECIFIC DIPEPTIDASE WITH A DINUCLEAR METAL CE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Prolidases are ubiquitous enzymes involved in the degradation of proline peptides. In mammals, prolidases are essential for the recycling of proline required for collagen synthesis. We are seeking to solve the structures of both mammalian and bacterial prolidases, with a view to defining the basis of their specificity. The first prolidase for which we have suitable crystals has been isolated from the hyper-thermophile, P. furiosus. The active site of this enzyme is reported to contain a dinuclear cobalt center. Surprisingly data recorded at SSRL in 2000 showed unequivocally that the crystals contained zinc at the active site. We now seek to record data from crystals grown in the presence of inhibitors or substrate to help define the enzyme mechanism.