Consider the molecule depicted below bond length, charges, lone pairs of electrons, what is the expected behavior of this molecule towards the PRMT enzyme. Considering electronegativity, chemical NH2 НО *H3Ñ HO NH2 ÕH
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PRMTs or Protein arginine methyltransferases are the enzymes that catalyzes arginine methylation in histone and the non-histone proteins. They are present in cytoplasm, nucleus and cell organelles. They can be classified into three types based on their ability to perform mono-methylation, asymmetric dimethylation or symmetric dimethylation. There are nine PRMTs identified in the human body.
The depicted structure is s-adenosyl methionine. They act as a substrate to the PRMTs. The PRMT transfers the methyl group from the S-adenosyl methionine and places it at guanidino nitrogen of arginine residue in the histone. The process occurs when lysine and arginine present in histone tail are attached to the PRMT catalytic site's SET site. This methylation process is vital because it could cause the changes in the protein-protein interaction of cell signalling, mRNA splicing, DNA repair etc.
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