TY  - JOUR
AU  - Konjik, Valentino
AU  - Brünle, Steffen
AU  - Demmer, Ulrike
AU  - Vanselow, Amanda
AU  - Sandhoff, Roger
AU  - Ermler, Ulrich
AU  - Mack, Matthias
TI  - The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes.
JO  - Angewandte Chemie / International edition
VL  - 56
IS  - 4
SN  - 1433-7851
CY  - Weinheim
PB  - Wiley-VCH
M1  - DKFZ-2017-00095
SP  - 1146 - 1151
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:27981706
DO  - DOI:10.1002/anie.201610292
UR  - https://inrepo02.dkfz.de/record/119340
ER  -