Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters.
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.
Brubaker
M J
MJ
Department of Chemistry, Wichita State University, Kansas 67208.
Groutas
W C
WC
Hoidal
J R
JR
Rao
N V
NV
D000595:Amino Acid Sequence; D001665:Binding Sites; D004952:Esters / Q000378:metabolism; D008969:Molecular Sequence Data; D053146:Myeloblastin; D009504:Neutrophils / Q000201:enzymology*; D010455:Peptides / Q000378:metabolism; D010636:Phenols / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds
D004952:Esters; D010455:Peptides; D010636:Phenols; D013438:Sulfhydryl Compounds; C042983:thiophenol; D012697:Serine Endopeptidases; D053146:Myeloblastin