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000119340 0247_ $$2ISSN$$a1521-3773
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000119340 037__ $$aDKFZ-2017-00095
000119340 041__ $$aeng
000119340 082__ $$a540
000119340 1001_ $$aKonjik, Valentino$$b0
000119340 245__ $$aThe Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes.
000119340 260__ $$aWeinheim$$bWiley-VCH$$c2017
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000119340 520__ $$a8-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.
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000119340 7001_ $$aBrünle, Steffen$$b1
000119340 7001_ $$aDemmer, Ulrike$$b2
000119340 7001_ $$aVanselow, Amanda$$b3
000119340 7001_ $$0P:(DE-He78)a928ded2085c8911822370cad0b4a728$$aSandhoff, Roger$$b4$$udkfz
000119340 7001_ $$aErmler, Ulrich$$b5
000119340 7001_ $$0http://orcid.org/0000-0002-7753-2422$$aMack, Matthias$$b6
000119340 773__ $$0PERI:(DE-600)2011836-3$$a10.1002/anie.201610292$$gVol. 56, no. 4, p. 1146 - 1151$$n4$$p1146 - 1151$$tAngewandte Chemie / International edition$$v56$$x1433-7851$$y2017
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