S-Catechol O-Methyltransferase (human, recombinant)

S-Catechol-O-methyltransferase (S-COMT) is the soluble cytosolic form of COMT.¹ A rough endoplasmic reticulum membrane-bound form of COMT (MB-COMT) is also encoded by the COMT gene but produced via a separate promoter and contains an additional 50 amino acid residues, which compose the membrane anchor region.^1,2 COMT is comprised of one domain with eight α helices surrounding a central β sheet.³ It is the methyltransferase responsible for transferring a methyl group from S-adenosyl-L-methionine (SAM) to a catechol hydroxyl in the inactivation or degradation of catechol-containing molecules such as catecholamines.⁴ S-COMT is involved primarily in the inactivation of endogenous and xenobiotic catechols, such as catechol-containing hormones and carcinogenic flavonoids, and MB-COMT is involved primarily in the degradation of endogenous catecholamine neurotransmitters.^4,5 S-COMT is the predominant form of COMT and is found primarily in the liver and kidney but is also found in the stomach, small intestine, adrenal gland, spleen, and brain.⁶ A valine-to-methionine substitution (Val158Met) in COMT affects its thermostability and may reduce its activity by greater than 50% in the human brain.⁷ The Val158Met variant of COMT is associated with Parkinson’s disease in an ethnicity-dependent manner.⁸ COMT interacts with severe acute respiratory coronavirus 2 (SARS-CoV-2) non-structural protein 7 (Nsp7), which, together with Nsp8, forms the primase complex of the replicase-transcriptase complex of SARS-CoV-2.⁹ Cayman’s S-Catechol-O-Methyltransferase (human, recombinant) protein can be used for ELISA, Western blot (WB), and enzyme activity assay applications.

WARNING This product is not for human or veterinary use.

1. Tilgmann, C., and Ulmanen, I. Purification methods of mammalian catechol-O-methyltransferases. J. Chromatogr. B Biomed. Appl. 684(1-2), 147-161 (1996).

2. Pedro, A.Q., Bonifácio, M.J., Queiroz, J.A., et al. A novel prokaryotic expression system for biosynthesis of recombinant human membrane-bound catechol-O-methyltransferase. J. Biotechnol. 156(2), 141-146 (2014).

3. Learmonth, D.A., Kiss, L.E., and Soares-da-Silva, P. The chemistry of catechol-O-methyltransferase inhibitors. Int. Rev. Neurobiol. 95, 119-162 (2010).

4. Lundström, K., Tenhunen, J., Tilgmann, C., et al. Cloning, expression and structure of catechol-O-methyltransferase. Biochim. Biophys. Acta 1251(1), 1-10 (1995).

5. Ma, Z., Liu, H., and Wu, B. Structure-based drug design of catechol-O-methyltransferase inhibitors for CNS disorders. Br. J. Clin. Pharmacol. 77(3), 410-420 (2014).

6. Karhunen, T., Tilgmann, C., Ulmanen, I., et al. Distribution of catechol-O-methyltransferase enzyme in rat tissues. J. Histochem. Cytochem. 42(8), 1079-1090 (1994).

7. Dickinson, D., and Elvevåg, B. Genes, cognition and brain through a COMT lens. Neuroscience 164(1), 72-87 (2009).

8. Wang, Y., Zou, Y., Xiao, J., et al. COMT Val158Met polymorphism and Parkinson’s disease risk: A pooled analysis in different populations. Neurol. Res. 41(4), 319-325 (2019).

9. Gordon, D.E., Jang, G.M., Bouhaddou, M., et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 583(7816), 459-468 (2020).