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conferenceseries
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Volume 8
Journal of Biotechnology & Biomaterials
ISSN: 2155-952X
Biotech Congress 2018 & Enzymology 2018
March 05-07, 2018
JOINT EVENT
20
th
Global Congress on
Biotechnology
3
rd
International Conference on
Enzymology and Molecular Biology
&
March 05-07, 2018 London, UK
The transient kinetic mechanism of protein arginine methylation
Y George Zheng
University of Georgia, USA
P
rotein arginine methyltransferases (PRMTs) catalyze the transfer of the methyl group from S-adenosyl-L-methionine
(AdoMet) to the guanidino group of arginine residues in protein substrates, resulting in mono and di-methylarginine
residues. Protein arginine methylation is an important posttranslational modification mark regulating epigenetics and
many other cellular pathways. We sought to resolve significant kinetic steps of PRMT catalysis by combining steady-state
and transient kinetics techniques. We have constructed a novel turnover model which reveals critical information about the
ternary complex formation and methyl transfer process. Methyl transfer was found to be the rate limiting step. Significantly,
the catalysis is found to follow a unique mechanism in which PRMT1 is able to randomly bind AdoMet or peptide substrate
to form binary complex but follows a kinetically preferred (ordered) pathway to form the ternary complex. The delineation of
PRMT1 transient kinetic mechanism provides new insights to understand biological function of arginine methylation and to
design potent PRMT inhibitors.
yzheng@uga.eduJ Biotechnol Biomater 2018, Volume 8
DOI: 10.4172/2155-952X-C2-092