Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters
Brubaker, Michael J.
Groutas, William C.
Hoidal, John R.
Rao, Narayanam V.
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Biochemical and biophysical research communications. 1992 Nov 16; 188(3): 1318-24.
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.
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