Catalysis by human leukocyte elastase. Role of secondary-subsite interactions

This publication has 23 references indexed in Scilit:

• Studies on reactivity of human leukocyte elastase, cathepsin G, and porcine pancreatic elastase toward peptides including sequences related to the reactive site of .alpha.1-protease inhibitor (.alpha.1-antitrypsin)
  Biochemistry, 1980
• Protonic reorganization and substrate structure in catalysis by serine proteases
  Journal of the American Chemical Society, 1980
• Steady-state kinetics of plasmin- and trypsin-catalysed hydrolysis of a number of tripeptide-p-nitroanilides
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1979
• Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.
  Journal of Biological Chemistry, 1979
• Catalysis and leaving group binding in anilide hydrolysis by chymotrypsin
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1978
• Substrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyte
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1977
• Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer
  Biochemistry, 1976
• The Kinetics of Hydrolysis of some Extended N-Aminoacyl-L-lysine Methyl Esters by Bovine alpha and beta-Trypsins
  European Journal of Biochemistry, 1976
• Acylation of subtilisin Carlsberg by phenyl esters.
  Journal of Biological Chemistry, 1976
• The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate^*
  Biochemistry, 1962