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- W2896050864 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 KM. The median values for PRMT turnover number (kcat) and catalytic efficiency (kcat/KM) are 0.0051 s−1 and 708 M−1 s−1, 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 kcat and kcat/KM 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." @default.
- W2896050864 created "2018-10-26" @default.
- W2896050864 creator A5000864648 @default.
- W2896050864 creator A5075824861 @default.
- W2896050864 date "2019-03-01" @default.
- W2896050864 modified "2023-09-27" @default.
- W2896050864 title "Evaluation of kinetic data: What the numbers tell us about PRMTs" @default.
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- W2896050864 doi "https://doi.org/10.1016/j.bbapap.2018.10.010" @default.
- W2896050864 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30342239" @default.
- W2896050864 hasPublicationYear "2019" @default.
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