ArticleInterdisciplinary sciences, computational life sciences2022
Computational Study of Methionine Methylation Process Catalyzed by SETD3.
Article in Interdisciplinary sciences, computational life sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The SETD3 enzyme has been identified as the methyltransferase for the His73 methylation in β-actin, and such methylation plays an important role in regulating the actin's biochemical properties and fine-tuning the protein's cellular roles. Further studies have demonstrated that SETD3 may be able to methylase some other residues, including lysine and methionine, that substitute His73 in the β-actin peptide. The activity of SETD3 on the Met73 peptide is low without turnover. Interestingly, it has been shown that the N255V and N255A mutations of SETD3 can increase the activity by about 3-fold for the methionine methylation, while such mutations lead to a significant reduction of k
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