Horse Urinary Kallikrein, II. Effect of Subsite Interactions on its Catalytic Activity
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm3.1988.369.1.397/pdf
Reference11 articles.
1. Refined 2 Å X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase
2. Individual Reaction Steps in the Release of Kallidin from Kininogen by Tissue Kallikrein
3. On the size of the active site in proteases. I. Papain
4. Tetrapeptide Substrates for the Discrimination among Kallikreins and other Trypsin-Like Serine Proteinases
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1. Selective Inhibitors of the Serine Protease Plasmin: Probing the S3 and S3‘ Subsites Using a Combinatorial Library;Journal of Medicinal Chemistry;2005-10-11
2. Differences in substrate and inhibitor sequence specificity of human, mouse and rat tissue kallikreins;Biochemical Journal;2004-06-15
3. Mapping of Human Plasma Kallikrein Active Site by Design of Peptides Based on Modifications of a Kazal-Type Inhibitor Reactive Site;Journal of Protein Chemistry;2003-08
4. Kinetic Peculiarities of Human Tissue Kallikrein: 1—Substrate Activation in the Catalyzed Hydrolysis of H--Valyl--leucyl--arginine 4-Nitroanilide and H--Valyl--leucyl--lysine 4-Nitroanilide; 2—Substrate Inhibition in the Catalyzed Hydrolysis of Nα-p-Tosyl--arginine Methyl Ester;Archives of Biochemistry and Biophysics;2002-04
5. Human Tissue Kallikrein S1 Subsite Recognition of Non-Natural Basic Amino Acids;Biochemistry;2001-04-04
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