title: (2S,3S)-Oxirane-2,3-dicarboxylic acid: a privileged platform for probing human cysteine cathepsins.
abstract: The notion that human cysteine cathepsins contribute only to general protein turnover within the lysosomes has changed in the last decade in a substantial manner. A continuously growing number of data accumulated in different fields of life sciences revealed that these enzymes are involved in a variety of pivotal physiological processes. To investigate these particular fraction of proteolytical activity of the human degradome even in a complex cellular environment, chemical probes that covalently label the corresponding proteases proved to be versatile tools. (2S,3S)-Oxirane-2,3-dicarboxylic acid provides an ideal platform for the design of such probing systems. Depending on the complexity of the attached recognition elements, either the activity of the entire group of human cysteine cathepsins or individual members can be detected.
authors.affiliation: Fakultät für Chemie, Universität Bielefeld, Universitätsstrasse 25, D-33615 Bielefeld, Germany. norbert.schaschke@uni-bielefeld.de
authors.forename: Norbert
authors.initials: N
authors.lastname: Schaschke
mesh_terms: D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000502:physiology; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000502:physiology; D003998:Dicarboxylic Acids / Q000737:chemistry*; D005027:Ethylene Oxide / Q000031:analogs & derivatives* / Q000737:chemistry; D006801:Humans; D040901:Proteomics / Q000379:methods*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity / Q000502:physiology
chemical_list: C520314:(2S,3S)-oxirane-2,3-dicarboxylic acid; D003998:Dicarboxylic Acids; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D005027:Ethylene Oxide