Identification of a Unique Radical S-Adenosylmethionine Methylase Likely Involved in Methanopterin Biosynthesis in Methanocaldococcus jannaschii

@article{Allen2014IdentificationOA,
  title={Identification of a Unique Radical S-Adenosylmethionine Methylase Likely Involved in Methanopterin Biosynthesis in Methanocaldococcus jannaschii},
  author={Kylie D. Allen and H. Xu and Robert H White},
  journal={Journal of Bacteriology},
  year={2014},
  volume={196},
  pages={3315 - 3323}
}
ABSTRACT Methanopterin (MPT) and its analogs are coenzymes required for methanogenesis and methylotrophy in specialized microorganisms. The methyl groups at C-7 and C-9 of the pterin ring distinguish MPT from all other pterin-containing natural products. However, the enzyme(s) responsible for the addition of these methyl groups has yet to be identified. Here we demonstrate that a putative radical S-adenosyl-l-methionine (SAM) enzyme superfamily member encoded by the MJ0619 gene in the… Expand
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It is shown that a unique Radical S-adenosyl-L-methionine (SAM) methyltransferase is required for the methylation of the arginine residue in the last and methane-releasing step of methanogenesis, which carries several exceptional posttranslational amino acid modifications. Expand
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TLDR
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TLDR
This review will highlight the most recent advances in the identification and characterization of radical SAM enzymes that harbor auxiliary iron-sulfur clusters. Expand
Evaluation of Pterin, a Promising Drug Candidate from Cyanide Degrading Bacteria
TLDR
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