Bauhinia proteinase inhibitor-based synthetic fluorogenic substrates for enzymes isolated from insect midgut and caterpillar bristles

Bauhinia proteinase inhibitor-based synthetic fluorogenic substrates for enzymes isolated from insect midgut and caterpillar bristles

Author Andrade, S. A. Google Scholar
Santomauro-Vaz, E. M. Google Scholar
Lopes, A. R. Google Scholar
Chudzinski-Tavassi, A. M. Google Scholar
Juliano, M. A. Google Scholar
Terra, W. R. Google Scholar
Sampaio, M. U. Google Scholar
Sampaio, CAM Google Scholar
Oliva, MLV Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Inst Butantan
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 trypsinlike enzyme activities, especially nonmammalian enzymes.
Keywords factor Xa
kallikrein
Kunitz inhibitor
Lonomia obliqua
plant
quenched fluorogenic substrates
sequence
serine proteinase inhibitor
Language English
Date 2003-03-01
Published in Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 384, n. 3, p. 489-492, 2003.
ISSN 1431-6730 (Sherpa/Romeo, impact factor)
Publisher Walter de Gruyter & Co
Extent 489-492
Origin http://dx.doi.org/10.1515/BC.2003.055
Access rights Closed access
Type Article
Web of Science ID WOS:000181664600018
URI http://repositorio.unifesp.br/handle/11600/27176

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