Abstract:
:The puromycin-sensitive aminopeptidase (ApPS) is a zinc metallopeptidase involved in the degradation of neuropeptides. Putative catalytic residues of the enzyme, Cys146, Glu338, and Lys396 were mutated, and the resultant mutant enzymes characterized. ApPS C146S exhibited normal catalytic activity, ApPS E338A exhibited decreased substrate binding, and ApPS K396I exhibited decreases in both substrate binding and catalysis. ApPS K396I and ApPS Y394F were analyzed with respect to transition state inhibitor binding. No effect was seen with the K396I mutation, but ApPS Y394F exhibited a 3.3-fold lower affinity for RB-3014, a transition state inhibitor, indicating that Tyr394 is involved in transition state stabilization.
journal_name
Peptidesjournal_title
Peptidesauthors
Thompson MW,Hersh LBdoi
10.1016/j.peptides.2003.07.012subject
Has Abstractpub_date
2003-09-01 00:00:00pages
1359-65issue
9eissn
0196-9781issn
1873-5169pii
S0196978103002778journal_volume
24pub_type
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