Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters

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Authors
Brubaker, Michael J.
Groutas, William C.
Hoidal, John R.
Rao, Narayanam V.
Advisors
Issue Date
1992-11-16
Type
Article
Keywords
Research Support, U.S. Gov't, P.H.S.
Research Projects
Organizational Units
Journal Issue
Citation
Biochemical and biophysical research communications. 1992 Nov 16; 188(3): 1318-24.
Abstract

A series of peptidyl thiobenzyl esters was used to map the active site of human leukocyte proteinase 3. The steady-state kinetics parameters reveal the following features regarding the substrate specificity of proteinase 3 and its putative active site: (a) the preferred P1 residue is a small hydrophobic amino acid such as aminobutyric acid, norvaline, valine or alanine (in decreasing order of preference); (b) the enzyme has an extended active site; and (c) its active site is similar to that of the related serine proteinases leukocyte elastase and leukocyte cathepsin G.

Table of Contents
Description
Full text of this article is not available in SOAR.
Publisher
Elsevier
Journal
Book Title
Series
Biochemical and biophysical research communications
Biochem. Biophys. Res. Commun.
PubMed ID
DOI
ISSN
0006-291X
EISSN