• Media type: E-Article
  • Title: A Cobalamin‐Dependent Radical SAM Enzyme Catalyzes the Unique Cα‐Methylation of Glutamine in Methyl‐Coenzyme M Reductase
  • Contributor: Gagsteiger, Jana; Jahn, Sören; Heidinger, Lorenz; Gericke, Lukas; Andexer, Jennifer N.; Friedrich, Thorsten; Loenarz, Christoph; Layer, Gunhild
  • Published: Wiley, 2022
  • Published in: Angewandte Chemie, 134 (2022) 32
  • Language: English
  • DOI: 10.1002/ange.202204198
  • ISSN: 1521-3757; 0044-8249
  • Origination:
  • Footnote:
  • Description: AbstractMethyl‐coenzyme M reductase, which is responsible for the production of the greenhouse gas methane during biological methane formation, carries several unique posttranslational amino acid modifications, including a 2‐(S)‐methylglutamine. The enzyme responsible for the Cα‐methylation of this glutamine is not known. Herein, we identify and characterize a cobalamin‐dependent radical SAM enzyme as the glutamine C‐methyltransferase. The recombinant protein from Methanoculleus thermophilus binds cobalamin in a base‐off, His‐off conformation and contains a single [4Fe‐4S] cluster. The cobalamin cofactor cycles between the methyl‐cob(III)alamin, cob(II)alamin and cob(I)alamin states during catalysis and produces methylated substrate, 5′‐deoxyadenosine and S‐adenosyl‐l‐homocysteine in a 1 : 1 : 1 ratio. The newly identified glutamine C‐methyltransferase belongs to the class B radical SAM methyltransferases known to catalyze challenging methylation reactions of sp3‐hybridized carbon atoms.