title: Transcreener: screening enzymes involved in covalent regulation.
abstract: Enzymes that catalyse group transfer reactions comprise a significant fraction of the human proteome and are a rich source of drug targets because of their role in covalent regulatory cycles. Phosphorylation, glycosylation, sulfonation, methylation and acetylation represent some of the key types of group transfer reactions that modulate the function of diverse biomolecules through covalent modification. Development of high-throughput screening methods for these enzymes has been problematic because of the diversity of acceptor substrates. Recently, the authors developed a novel assay platform called Transcreener that relies upon fluorescence detection of the invariant reaction product of a group transfer reaction, usually a nucleotide. This platform enables screening of any isoform in a family of group transfer enzymes, with any acceptor substrate, using the same assay reagents.
authors.affiliation: BellBrook Labs, 525 Science Drive, Suite 110, Madison, WI 53711, USA. bob.lowery@bellbrooklabs.com
authors.forename: Robert G
authors.initials: RG
authors.lastname: Lowery
authors.forename: Karen
authors.initials: K
authors.lastname: Kleman-Leyer
mesh_terms: D000818:Animals; D016503:Drug Delivery Systems / Q000379:methods*; D004353:Drug Evaluation, Preclinical / Q000295:instrumentation / Q000379:methods; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry* / Q000502:physiology*; D005454:Fluorescence Polarization / Q000295:instrumentation* / Q000379:methods*; D006801:Humans; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D013379:Substrate Specificity / Q000502:physiology
chemical_list: D004791:Enzyme Inhibitors; D004798:Enzymes; D011494:Protein Kinases