Abstract
In the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor, 6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol (1) is 3-methylated to form 2, then 4-guanylylated to form 3, and converted into the full cofactor. HcgA-G proteins catalyze the biosynthetic reactions. Herein, we report the function of two radical S-adenosyl methionine enzymes, HcgA and HcgG, as uncovered by in vitro complementation experiments and the use of purified enzymes. In vitro biosynthesis using the cell extract from the Methanococcus maripaludis ΔhcgA strain was complemented with HcgA or precursors 1, 2 or 3. The results suggested that HcgA catalyzes the biosynthetic reaction that forms 1. We demonstrated the formation of 1 by HcgA using the 3 kDa cell extract filtrate as the substrate. Biosynthesis in the ΔhcgG system was recovered by HcgG but not by 3, which indicated that HcgG catalyzes the reactions after the biosynthesis of 3. The data indicated that HcgG contributes to the formation of CO and completes biosynthesis of the FeGP cofactor.
Original language | English (US) |
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Article number | e202213239 |
Journal | Angewandte Chemie - International Edition |
Volume | 61 |
Issue number | 50 |
DOIs | |
State | Published - Dec 12 2022 |
Bibliographical note
Publisher Copyright:© 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.
Keywords
- Acyl Ligands
- Biosynthesis
- FeGP Cofactor
- Radical S-Adenosyl Methionine Enzymes
- [Fe]-Hydrogenase
PubMed: MeSH publication types
- Journal Article
- Research Support, Non-U.S. Gov't