Analysis of conserved residues of the human puromycin-sensitive aminopeptidase.
作者： Michael W. Thompson , Louis B. Hersh
DOI: 10.1016/J.PEPTIDES.2003.07.012
关键词:
摘要: The puromycin-sensitive aminopeptidase (ApPS) is a zinc metallopeptidase involved in the degradation of neuropeptides. Putative catalytic residues enzyme, Cys146, Glu338, and Lys396 were mutated, resultant mutant enzymes characterized. ApPS C146S exhibited normal activity, E338A decreased substrate binding, K396I decreases both binding catalysis. Y394F analyzed with respect to transition state inhibitor binding. No effect was seen mutation, but 3.3-fold lower affinity for RB-3014, inhibitor, indicating that Tyr394 stabilization.
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