Catalysis by human leukocyte elastase: III. Steady-state kinetics for the hydrolysis of p-nitrophenyl esters
- 1 February 1985
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 236 (2), 677-680
- https://doi.org/10.1016/0003-9861(85)90673-3
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Active site mapping of the serine proteases human leukocyte elastase, cathepsin G, porcine pancreatic elastase, rat mast cell proteases I and II, bovine chymotrypsin A.alpha., and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester substratesBiochemistry, 1984
- Catalysis by human leukocyte elastase. Rate-limiting deacylation for specific p-nitroanilides and amidesJournal of the American Chemical Society, 1984
- Catalysis by human leukocyte elastase: substrate structural dependence of rate-limiting protolytic catalysis and operation of the charge relay systemJournal of the American Chemical Society, 1983
- Correlative variations in enzyme-derived and substrate-derived structures of catalytic transition states. Implications for the catalytic strategy of acyl-transfer enzymesJournal of the American Chemical Society, 1983
- Mapping of the substrate-binding site of the human granulocyte elastase by the aid of tripeptidyl-p-nitroanilide substratesBiochemical and Biophysical Research Communications, 1980
- 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 proteasesJournal of the American Chemical Society, 1980
- Serine Proteases: Structure and Mechanism of CatalysisAnnual Review of Biochemistry, 1977
- Substrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyteBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967