ChemBioChem

Cover image for Vol. 18 Issue 24

Editor: Ruben Ragg; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

Associated Title(s): ChemCatChem, ChemMedChem, ChemPhysChem, ChemSusChem

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December 14, 2017

Very Important Paper: Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism

Jennifer I. Brown, Timo Koopmans, Jolinde van Strien, Nathaniel I. Martin,* Adam Frankel*

Very Important Paper: Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism Jennifer I. Brown, Timo Koopmans, Jolinde van Strien, Nathaniel I. Martin,* Adam Frankel*Protein arginine N-methyltransferases (PRMTs) are mechanistically complex. Published reports indicate that PRMTs demonstrate variable dimethylation processivity. Results also dispute whether these enzymes bind their target and cofactor substrates randomly or sequentially. Here, N.I. Martin (University of Utrecht, Netherlands), A. Frankel (University of British Columbia, Canada) and co-workers offer a comprehensive literature review and propose explanations for the disparities within the field. They demonstrate that PRMT1 processivity depends on both cofactor and enzyme concentration, indicating that experimental design profoundly affects substrate dimethylation. Furthermore, they show that PRMT1 binds its substrates using a sequential ordered Bi--Bi mechanism. Considering the structural and functional conservation among PRMTs, these insights likely extend throughout the PRMT family.

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