Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity. Issue 2 (8th January 2017)

• Record Type: Journal Article
• Authors: Siegrist, Jutta; Netzer, Julia; Mordhorst, Silja; Karst, Lukas; Gerhardt, Stefan; Einsle, Oliver; Richter, Michael; Andexer, Jennifer N.
• Is Part Of: FEBS letters. Volume 591:Issue 2(2017)
• Page Start: 312
• Page End: 321
• Publication Date: 2017-01-08
• Subjects: biocatalysis -- catechol -- catechol‐O‐methyltransferase -- methylation -- SafC -- structure–function relationship; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12530
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Abstract : Mg 2+ ‐dependent catechol‐ O ‐methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial Mx SafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of Mx SafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol‐ O ‐methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.