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β‐Lactones as Privileged Structures for the Active‐Site Labeling of Versatile Bacterial Enzyme Classes
Author(s) -
Böttcher Thomas,
Sieber Stephan A.
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200705768
Subject(s) - computational biology , enzyme , proteome , function (biology) , identification (biology) , protein function , computer science , natural product , chemistry , biochemistry , combinatorial chemistry , biology , gene , microbiology and biotechnology , ecology
A chemical proteomic strategy has been applied directly to bacterial proteomes, and β‐lactones have been identified as important natural product derivatives with a high affinity to various enzyme classes (see picture). This approach may serve as a potent tool for the identification of novel antibacterial targets, the study of their function, and the definition of novel lead structures for the design of enzyme inhibitors.