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Bauhinia Proteinase Inhibitor-Based Synthetic Fluorogenic Substrates for Enzymes Isolated from Insect Midgut and Caterpillar Bristles
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S.A. Andrade
Published/Copyright:
June 1, 2005
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.
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Published Online: 2005-06-01
Published in Print: 2003-03-14
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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