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

    Date
    1992-11-16
    Author
    Brubaker, Michael J.
    Groutas, William C.
    Hoidal, John R.
    Rao, Narayanam V.
    Metadata
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    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.
    Description
    Full text of this article is not available in SOAR.
    URI
    http://hdl.handle.net/10057/4290
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