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

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 Chem

journal_title

Biological chemistry

authors

Andrade SA,Santomauro-Vaz EM,Lopes AR,Chudzinski-Tavassi AM,Juliano MA,Terra WR,Sampaio MU,Sampaio CA,Oliva ML

doi

10.1515/BC.2003.055

keywords:

subject

Has Abstract

pub_date

2003-03-01 00:00:00

pages

489-92

issue

3

eissn

1431-6730

issn

1437-4315

journal_volume

384

pub_type

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