ArticleScientific reports2019
Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 29 citations in OpenAlex.
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- Characterization of two O-methyltransferases involved in the biosynthesis of O-methylated catechins in tea plant.Nature communications · 2023Article
- Structome: a tool for the rapid assembly of datasets for structural phylogenetics.Bioinformatics advances · 2023Article
- Expanding the eukaryotic genetic code with a biosynthesized 21st amino acid.Protein science : a publication of the Protein Society · 2022Article
- Mycobacterium tuberculosis requires SufT for Fe-S cluster maturation, metabolism, and survival in vivo.PLoS pathogens · 2022Article
- Article
- The Gut Microbiota Impact Cancer Etiology through "Phase IV Metabolism" of Xenobiotics and Endobiotics.Cancer prevention research (Philadelphia, Pa.) · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Catechol O-methyltransferase (COMT) is widely distributed in nature and installs a methyl group onto one of the vicinal hydroxyl groups of a catechol derivative. Enzymes belonging to this family require two cofactors for methyl transfer: S-adenosyl-l-methionine as a methyl donor and a divalent metal cation for regiospecific binding and activation of a substrate. We have determined two high-resolution crystal structures of Rv0187, one of three COMT paralogs from Mycobacterium tuberculosis, in the presence and absence of cofactors. The cofactor-bound structure clearly locates strontium ions and S-adenosyl-l-homocysteine in the active site, and together with the complementary structure of the ligand-free form, it suggests conformational dynamics induced by the binding of cofactors. Examination of in vitro activities revealed promiscuous substrate specificity and relaxed regioselectivity against various catechol-like compounds. Unexpectedly, mutation of the proposed catalytic lysine residue did not abolish activity but altered the overall landscape of regiospecific methylation.
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