title: Sbustrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyte.
abstract: Human granulocyte elastase (EC 3.4.21.11) differs from hog pancreatic elastase in its specificity for synthetic substrates. Although hydrolyzing peptide bonds adjacent to the carboxyl group of alanine, the granulocyte enzyme prefers valine at the cleaved bond, in contrast to the pancreatic enzyme which prefers alanine. Peptide bonds involving the carboxyl group of isoleucine can be hydrolyzed by the granulocyte enzyme but are not hydrolyzed to any significant extent extent by pancreatic elastase. This difference in specificty could explain the lower sensitivity of the granulocyte enzyme to inhibitors containing alanine analogs, such as the peptide chloromethyl ketones and elastatinal. The human granulocyte chymotrypsin-like enzyme differs from pancreatic chymotrypsin by being able to cleave substrates containing leucine in addition to those containing the aromatic amino acids.
mesh_terms: D000818:Animals; D002918:Chymotrypsin / Q000097:blood*; D003594:Cytoplasmic Granules / Q000201:enzymology; D004285:Dogs; D006098:Granulocytes / Q000201:enzymology*; D000882:Haplorhini; D006801:Humans; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D009928:Organ Specificity; D010179:Pancreas / Q000201:enzymology; D010196:Pancreatic Elastase / Q000097:blood* / Q000378:metabolism; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013552:Swine
chemical_list: D002918:Chymotrypsin; D010196:Pancreatic Elastase