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Functional and Kinetic Characterization of the Human Post-proline Cleaving Enzyme Prolyl Oligopeptidase

David Ruiz Carrillo

出版	2009
URL	http://books.google.com.hk/books?id=bi2uXwAACAAJ&hl=&source=gbs_api

註釋

Prolyl endopeptidase (PEP; EC 3.4.21.26) is a cytosolic 80kDa monomeric serine peptidase targeting mainly proline containing peptides. Recombinant human PEP variants were generated to characterize relevant residues involved in the architecture of the S1-S3 active site pockets. Steady-state kinetics and MALDI-TOF mass spectrometry were used to draw a complete profile of PEP catalytic properties. Our characterization allowed us to unveil the enzyme's post-cysteine specificity and confirmed the critical relevance of residues R643 and W595 on the enzyme's catalytic mechanism.