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Noncompetitive Inhibitor of Thrombin
Author(s) -
Koh Cho Yeow,
Kazimirova Maria,
Nuttall Patricia A.,
Kini R. Manjunatha
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900371
Subject(s) - thrombin , proteolysis , non competitive inhibition , chemistry , discovery and development of direct thrombin inhibitors , substrate (aquarium) , biochemistry , enzyme inhibition , stereochemistry , active site , enzyme , pharmacology , biology , platelet , immunology , ecology
Two for the price of one : Full length variegin competitively inhibits thrombin in a substrate‐like fashion. Upon proteolysis, the cleaved fragment is able to inhibit thrombin noncompetitively; this results in overall prolonged and potent inhibition. This is the first account of a potent and specific classical noncompetitive inhibitor of the thrombin active site, and is unlike other cleavable substrates or inhibitors of thrombin.