%0 Journal Article
%A Konjik, Valentino
%A Brünle, Steffen
%A Demmer, Ulrike
%A Vanselow, Amanda
%A Sandhoff, Roger
%A Ermler, Ulrich
%A Mack, Matthias
%T The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes.
%J Angewandte Chemie / International edition
%V 56
%N 4
%@ 1433-7851
%C Weinheim
%I Wiley-VCH
%M DKFZ-2017-00095
%P 1146 - 1151
%D 2017
%X 8-demethyl-8-aminoriboflavin-5'-phosphate (AFP) synthase (RosB) catalyzes the key reaction of roseoflavin biosynthesis by forming AFP from riboflavin-5'-phosphate (RP) and glutamate via the intermediates 8-demethyl-8-formylriboflavin-5'-phosphate (OHC-RP) and 8-demethyl-8-carboxylriboflavin-5'-phosphate (HO2 C-RP). To understand this reaction in which a methyl substituent of an aromatic ring is replaced by an amine we structurally characterized RosB in complex with OHC-RP (2.0 Å) and AFP (1.7 Å). RosB is composed of four flavodoxin-like subunits which have been upgraded with specific extensions and a unique C-terminal arm. It appears that RosB has evolved from an electron- or hydride-transferring flavoprotein to a sophisticated multi-step enzyme which uses RP as a substrate (and not as a cofactor). Structure-based active site analysis was complemented by mutational and isotope-based mass-spectrometric data to propose an enzymatic mechanism on an atomic basis.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:27981706
%R 10.1002/anie.201610292
%U https://inrepo02.dkfz.de/record/119340