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  The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes

Konjik, V., Brünle, S., Demmer, U., Vanselow, A., Sandhoff, R., Ermler, U., et al. (2017). The Crystal Structure of RosB: Insights into the Reaction Mechanism of the First Member of a Family of Flavodoxin-like Enzymes. Angewandte Chemie, International Edition in English, 56(4), 1146-1151. doi:10.1002/anie.201610292.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-27D9-F Version Permalink: https://hdl.handle.net/21.11116/0000-0002-EB39-6
Genre: Journal Article

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 Creators:
Konjik, Valentino1, Author
Brünle, Steffen2, Author           
Demmer, Ulrike2, Author           
Vanselow, Amanda1, Author
Sandhoff, Roger3, Author
Ermler, Ulrich2, Author           
Mack, Matthias1, Author
Affiliations:
1Mannheim University of Applied Sciences Paul-Wittsack-Strasse 10, 68163 Mannheim, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3German Cancer Research Center (DKFZ), Im Neuenheimer Feld 280, 69120 Heidelberg, Germany, ou_persistent22              

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 Abstract: 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 (HO2C-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 (2.0Å) and AFP (1.7Å). 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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Language(s): eng - English
 Dates: 2016-10-202016-12-162017-01-19
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201610292
 Degree: -

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Title: Angewandte Chemie, International Edition in English
  Other : Angewandte Chemie International Edition in English
  Other : Angew. Chem., Int. Ed. Engl.
  Other : Angew. Chem. Int. Ed. Engl.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 56 (4) Sequence Number: - Start / End Page: 1146 - 1151 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833