Kinetic mechanism of protein arginine methyltransferase 6 (PRMT6).
Obianyo, Obiamaka ; Thompson, Paul R
Citations
Authors
Student Authors
Faculty Advisor
Academic Program
UMass Chan Affiliations
Document Type
Publication Date
Subject Area
Embargo Expiration Date
Link to Full Text
Abstract
The protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the mono- and dimethylation of arginine residues in a variety of proteins. Although these enzymes play important roles in a variety of cellular processes, aberrant PRMT activity is associated with several disease states, including heart disease and cancer. In an effort to guide the development of inhibitors targeting individual PRMTs, we initiated studies to characterize the molecular mechanisms of PRMT catalysis. Herein, we report studies on the kinetic mechanism of PRMT6. Initial velocity, product inhibition, and dead-end analog inhibition studies with the AcH4-21 and R1 peptides, as well as their monomethylated versions, indicate, in contrast to a previous report, that PRMT6 utilizes a rapid equilibrium random mechanism with dead-end EAP and EBQ complexes.
Source
J Biol Chem. 2012 Feb 17;287(8):6062-71. doi: 10.1074/jbc.M111.333609. Epub 2012 Jan 3. Link to article on publisher's site
Year of Medical School at Time of Visit
Sponsors
Dates of Travel
DOI
Permanent Link to this Item
PubMed ID
Other Identifiers
Notes
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.