| Home > Publications database > The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes. > print |
| 001 | 119340 | ||
| 005 | 20240228145433.0 | ||
| 024 | 7 | _ | |2 doi |a 10.1002/anie.201610292 |
| 024 | 7 | _ | |2 pmid |a pmid:27981706 |
| 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 |a article |
| 336 | 7 | _ | |2 DataCite |a Output Types/Journal article |
| 336 | 7 | _ | |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |a Journal Article |b journal |m journal |s 1511333212_28941 |
| 336 | 7 | _ | |2 BibTeX |a ARTICLE |
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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 |
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