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024 7 _ |2 doi
|a 10.1002/anie.201610292
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024 7 _ |2 ISSN
|a 0044-8249
024 7 _ |2 ISSN
|a 0570-0833
024 7 _ |2 ISSN
|a 1433-7851
024 7 _ |2 ISSN
|a 1521-3773
024 7 _ |a altmetric:14836323
|2 altmetric
037 _ _ |a DKFZ-2017-00095
041 _ _ |a eng
082 _ _ |a 540
100 1 _ |a Konjik, Valentino
|b 0
245 _ _ |a The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes.
260 _ _ |a Weinheim
|b Wiley-VCH
|c 2017
336 7 _ |2 DRIVER
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520 _ _ |a 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.
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700 1 _ |a Brünle, Steffen
|b 1
700 1 _ |a Demmer, Ulrike
|b 2
700 1 _ |a Vanselow, Amanda
|b 3
700 1 _ |0 P:(DE-He78)a928ded2085c8911822370cad0b4a728
|a Sandhoff, Roger
|b 4
|u dkfz
700 1 _ |a Ermler, Ulrich
|b 5
700 1 _ |0 http://orcid.org/0000-0002-7753-2422
|a Mack, Matthias
|b 6
773 _ _ |0 PERI:(DE-600)2011836-3
|a 10.1002/anie.201610292
|g Vol. 56, no. 4, p. 1146 - 1151
|n 4
|p 1146 - 1151
|t Angewandte Chemie / International edition
|v 56
|x 1433-7851
|y 2017
909 C O |o oai:inrepo02.dkfz.de:119340
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910 1 _ |0 I:(DE-588b)2036810-0
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914 1 _ |y 2017
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