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  Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis

Fujishiro, T., Bai, L., Xu, T., Xie, X., Schick, M., Kahnt, J., et al. (2016). Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis. Angewandte Chemie International Edition in English, 55(33), 9648-9651. doi:10.1002/anie.201604352.

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 Creators:
Fujishiro, Takashi1, Author              
Bai , Liping1, Author
Xu , Tao2, Author
Xie , Xiulan3, Author
Schick, Michael1, Author
Kahnt, Jörg1, Author              
Rother, Michael4, Author
Hu , Xile2, Author
Ermler, Ulrich5, Author              
Shima, Seigo1, 6, Author              
Affiliations:
1Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Straße 10, 35043 Marburg, ou_persistent22              
2Institute of Chemical Science and Engineering Ecole Polytechnique Fédérale de Lausanne (EPFL) ISIC-LSCI, BCH 3305, 1015 Lausanne (Switzerland, ou_persistent22              
3Department of Chemistry, Philipps Universität Marburg, Hans-Meerwein-Straße, 35032 Marburg (Germany), ou_persistent22              
4Institut für Mikrobiologie, Technische Universität Dresden, 01062 Dresden (Germany), ou_persistent22              
5Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
6PRESTO, Japan, Science and Technology Agency, JST Saitama 332-0012 (Japan), ou_persistent22              

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 Abstract: Previous retrosynthetic and isotope-labeling studies have indicated that biosynthesis of the iron guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase requires a methyltransferase. This hypothetical enzyme covalently attaches the methyl group at the 3-position of the pyridinol ring. We describe the identification of HcgC, a gene product of the hcgA-G cluster responsible for FeGP cofactor biosynthesis. It acts as an S-adenosylmethionine (SAM)-dependent methyltransferase, based on the crystal structures of HcgC and the HcgC/SAM and HcgC/S-adenosylhomocysteine (SAH) complexes. The pyridinol substrate, 6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol, was predicted based on properties of the conserved binding pocket and substrate docking simulations. For verification, the assumed substrate was synthesized and used in a kinetic assay. Mass spectrometry and NMR analysis revealed 6-carboxymethyl-3,5-dimethyl-4-hydroxy-2-pyridinol as the reaction product, which confirmed the function of HcgC

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Language(s): eng - English
 Dates: 2016-05-042016-08-032016-08-08
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201604352
 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: 55 (33) Sequence Number: - Start / End Page: 9648 - 9651 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833