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A Coupled Fluorescence-Based Assay for the Detection of Protein Arginine N-methyltransferase 6 (PRMT6) Enzymatic Activity

A Coupled Fluorescence-Based Assay for the Detection of Protein Arginine N-methyltransferase 6 (PRMT6) Enzymatic Activity

Jan Kramer, Veronika Désor, Steffen Brunst, Sandra K Wittmann, Jörn Lausen, Jan Heering, Anna Proschak, Ewgenij Proschak

Anal Biochem. 2018 Apr 15;547:7-13.

PMID: 29410016

Abstract:

The protein arginine N-methyltransferase 6 (PRMT6) is overexpressed in a variety of different cancer types and plays a role in human immunodeficiency virus (HIV) infections. Furthermore, the PRMT6 activity might also influence the pathogenesis of neurodegenerative, inflammatory, and cardiovascular diseases, whereby it becomes an interesting target for drug development. Previously reported activity assays for PRMT6 activity are either expensive, time-consuming or use radioactive substrates. To overcome these challenges, we developed a coupled fluorescence-based activity assay using recombinant PRMT6 expressed in E. coli. In the first step of the assay, the fluorogenic substrate Nα-Benzoyl-L-arginine-7-amido-4-methylcoumarin (Bz-Arg-AMC) is methylated by PRMT6, while in a second step the remaining un-methylated substrate is cleaved by trypsin, producing the fluorescent 7-amino-4-methylcoumarin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416087	PRMT6 human			Price

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