Evaluation of kinetic data: What the numbers tell us about PRMTs.

TitleEvaluation of kinetic data: What the numbers tell us about PRMTs.
Publication TypeJournal Article
Year of Publication2018
AuthorsFrankel A, Brown JI
JournalBiochim Biophys Acta Proteins Proteom
Volume1867
Issue3
Pagination306-316
Date Published10/2018
ISSN1878-1454
Abstract

Protein arginine N-methyltransferase (PRMT) kinetic parameters have been catalogued over the past fifteen years for eight of the nine mammalian enzyme family members. Like the majority of methyltransferases, these enzymes employ the highly ubiquitous cofactor S-adenosyl-l-methionine as a co-substrate to methylate arginine residues in peptidic substrates with an approximately 4-μM median K. The median values for PRMT turnover number (k) and catalytic efficiency (k/K) are 0.0051 s and 708 M s, respectively. When comparing PRMT metrics to entries found in the BRENDA database, we find that while PRMTs exhibit high substrate affinity relative to other enzyme-substrate pairs, PRMTs display largely lower k and k/K values. We observe that kinetic parameters for PRMTs and arginine demethylase activity from dual-functioning lysine demethylases are statistically similar, paralleling what the broader enzyme families in which they belong reveal, and adding to the evidence in support of arginine methylation reversibility.

DOI10.1016/j.bbapap.2018.10.010
Alternate JournalBiochim Biophys Acta Proteins Proteom
PubMed ID30342239