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Updated: Sep 20, 2025

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
Published on: August 7, 2021
Computational study revealed a "pull-push" radical transfer mechanism of Mmp10-catalyzed C-methylation of arginine
Wen-Hao Deng1, Rong-Zhen Liao1
1Key Laboratory of Material Chemistry for Energy Conversion and Storage, Ministry of Education, Hubei Key Laboratory of Bioinorganic Chemistry and Materia Medica, Hubei Key Laboratory of Materials Chemistry and Service Failure, School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, Wuhan 430074, P. R. China. rongzhen@hust.edu.cn.
Abstract:
Mmp10 is a B12-dependent SAM radical enzyme that catalyzes C-methylation of arginine. The quantum chemical cluster calculations of Mmp10 revealed a "pull-push" radical transfer mechanism in which a 5'-deoxyadenosine radical first abstracts a hydrogen atom from the arginine residue and then methylcobalamin donates a methyl group to the arginine residue. The stereoselectivity and regioselectivity of Mmp10 originated in a specific substrate binding mode enabled by the active site.
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