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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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ISSN
1437-4315
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Volume 384, Issue 3

Issues

Bauhinia Proteinase Inhibitor-Based Synthetic Fluorogenic Substrates for Enzymes Isolated from Insect Midgut and Caterpillar Bristles

S.A. Andrade / E.M. Santomauro-Vaz / A.R. Lopes / A.M. Chudzinski-Tavassi / M.A. Juliano / W.R. Terra / M.U. Sampaio / C.A.M. Sampaio / M.L.V. Oliva
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2003.055

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.

About the article

Published Online: 2005-06-01

Published in Print: 2003-03-14


Citation Information: Biological Chemistry, Volume 384, Issue 3, Pages 489–492, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2003.055.

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