Abstract:
:Bauhinia ungulata factor Xa inhibitor (BuXI) inactivates factor Xa and LOPAP, a prothrombin activator proteinase isolated from the venom of Lonomia obliqua caterpillar bristles. The reactive site of the enzyme-inhibitor interaction was explored to design specific substrates for both enzymes. Methionine is crucial for LOPAP and factor Xa substrate interaction, since the change of both Met residues in the substrates abolished the hydrolysis. Synthetic substrates containing the sequence around the reactive site of BbKI, a plasma kallikrein inhibitor, were shown to be specific for trypsin hydrolysis. Therefore, these substrates may be an alternative in studies aiming at a characterization of trypsin-like enzyme activities, especially non-mammalian enzymes.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Andrade SA,Santomauro-Vaz EM,Lopes AR,Chudzinski-Tavassi AM,Juliano MA,Terra WR,Sampaio MU,Sampaio CA,Oliva MLdoi
10.1515/BC.2003.055keywords:
subject
Has Abstractpub_date
2003-03-01 00:00:00pages
489-92issue
3eissn
1431-6730issn
1437-4315journal_volume
384pub_type
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