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Methyltransferase

Sino biological offers a comprehensive set of tools for research on methyltransferases, including recombinant proteins, antibodies (mouse mAbs, rabbit mAbs, and rabbit pAbs), ELISA kits, and ORF cDNA clones. Methyltransferases are a group of transferases that catalyze the transfer of a methyl group from a donor to an acceptor. Methylation usually occurs on nucleic bases in DNA or amino acids in protein structures. Methyltransferase uses a reactive methyl group bound to sulfur in S-adenosyl methionine (SAM) as the methyl donor. Excepted for DNA methyltransferase (DNMT) and histone methyltransferase (HMT), methyltransferases also include 5-methyltetrahydrofolate-homocysteine methyltransferase (MTR, MTRR), catechol-o-methyl transferases (COMT) and acetylserotonin o-methyltransferase (ASMT).

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Methyltransferase Background

Methyltransferases are a group of transferases that catalyze the transfer of a methyl group from a donor to an acceptor. Methylation usually occurs on nucleic bases in DNA or amino acids in protein structures. Methyltransferase uses a reactive methyl group bound to sulfur in S-adenosyl methionine (SAM) as the methyl donor. Excepted for DNA methyltransferase (DNMT) and histone methyltransferase (HMT), methyltransferases also include 5-methyltetrahydrofolate-homocysteine methyltransferase (MTR, MTRR), catechol-o-methyl transferases (COMT) and acetylserotonin o-methyltransferase (ASMT).

DNA methyltransferase transfers a methyl group to DNA, which is often used to silence and regulate genes without changing the original DNA sequence. Three active DNA methyltransferases have been identified in mammals: DNMT1, DNMT3A and DNMT3B. DNA methyltransferase catalyzed methylation, which occurs on cytosine residues, may be involved in cancer development. Hypermethylation of tumor suppressor genes is one of the most consistent hallmarks of human cancers. DNA methyltransferase inhibitors have shown significant clinical benefits, mostly in the therapy of leukemias.

Histone methyltransferases (HMT) are enzymes, including histone-lysine N-methyltransferase and histone-arginine N-methyltransferase, which catalyze the transfer of one to three methyl groups from the cofactor S-Adenosyl methionine to lysine or arginine residues of histone proteins. Arginine methylation can occur in the mono-methyl, symmetrical di-methyl or asymmetrical di-methyl state. Histone-lysine N-methyltransferases are a family of proteins that contain a SET domain. Each lysine amine group can be modified by the addition of one, two or three methyl groups. Recently a group of enzymes that antagonize or remove histone methylation have been identified. Histone methyltransferase plays important roles in regulating transcription, genome integrity and epigenetic inheritance.

Epigenetics, defined as heritable changes to the non-DNA sequence related heredity, is at the epicenter of modern medicine because it can help to explain the relationship between an individual’s genetic background, the environment, aging, and disease. The best known epigenetic marker is DNA methylation. DNA methylation occurs in a complex chromatin network and is influenced by the modifications in histone structure that are commonly disrupted in cancer cells. Therefore, re-expression of epigenetically silenced tumor suppressor genes is a rational strategy for the treatment of human cancers. Epigenetic modifiers like DNA methyltransferase (DNMT) inhibitors and histone deacteylase (HDAC) inhibitors induce the re-expression of epigenetically silenced genes in vitro and in vivo. And they demonstrate safety and efficacy against cancers in clinical trials.

Methyltransferase References

    1. Klose RJ, et al. (2008) Regulation of histone methylation by demethylimination and demethylation. Nat Rev Mol Cell Biol. 8(4):307-18.
    2. AP Feinberg (2008) Epigenetics at the Epicenter of Modern Medicine. JAMA. 299(11):1345-1350.
    3. M Esteller (2008) Epigenetics in Cancer. The New England Journal of Medicine 358:1148-59.
    4. Fandy TE (2009) Development of DNA methyltransferase inhibitors for the treatment of neoplastic diseases. Curr Med Chem. 16(17):2075-85.
    5. Spannhoff A, et al. (2009) The emerging therapeutic potential of histone methyltransferase and demethylase inhibitors. ChemMedChem. 4(10):1568-82.