Functional and structural characterisation of a bacterial O-methyltransferase and factors determining regioselectivity.

Abstract:

:Mg2+ -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 MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Siegrist J,Netzer J,Mordhorst S,Karst L,Gerhardt S,Einsle O,Richter M,Andexer JN

doi

10.1002/1873-3468.12530

subject

Has Abstract

pub_date

2017-01-01 00:00:00

pages

312-321

issue

2

eissn

0014-5793

issn

1873-3468

journal_volume

591

pub_type

信件
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