title: Activity-based proteomics probes for carbohydrate-processing enzymes: current trends and future outlook.
abstract: Carbohydrate-processing enzymes are gaining more attention due to their roles in health and disease as these enzymes are involved in the construction and deconstruction of vast arrays of glycan structures. As a result, the development of methods to identify these enzymes in complex biological systems is of increasing interest. Activity-based proteomics probes (ABPPs) are increasingly being used in glycobiology to detect and identify functionally related proteins (and homologues) within a biological system. This review will describe the design of activity-based proteomics probes, provide examples of compounds that have been used to profile activity in the area of carbohydrate-processing enzymes, and give some future perspectives.
authors.affiliation: School of Chemistry and Biochemistry, The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia. Electronic address: keith.stubbs@uwa.edu.au.
authors.forename: Keith A
authors.initials: KA
authors.lastname: Stubbs
mesh_terms: D000818:Animals; D054812:Cyclitols / Q000737:chemistry; D057075:Enzyme Assays; D005456:Fluorescent Dyes / Q000737:chemistry; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D016695:Glycosyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D006801:Humans; D040901:Proteomics; D011809:Quinones / Q000737:chemistry
chemical_list: D054812:Cyclitols; D005456:Fluorescent Dyes; D011809:Quinones; D016695:Glycosyltransferases; D006026:Glycoside Hydrolases
keywords: Activity-based proteomics probes; Carbohydrate-processing enzymes; Glycobiology; Glycoside hydrolases; Glycosyl transferases