White, Robert H. Identification of an Enzyme Catalyzing the Conversion of Sulfoacetaldehyde to 2‑Mercaptoethanesulfonic Acid in Methanogens Coenzyme M is an essential coenzyme for the biochemical production of methane. This Communication reports on the identification of an enzyme catalyzing the last step in the biosynthesis of coenzyme M in methanogens. Data presented here show that the enzyme, derived from mj1681, catalyzes the conversion of the aldehyde functional group of sulfoacetaldehyde into the thiol group of 2-mercaptoethanesulfonic acid. Thus, a putative coenzyme M synthase (comF) has similarities in sequence with both MJ0100 and MJ0099 proteins previously shown to be involved in the biosynthesis of homocysteine [Allen, K. D., et al. (2015) <i>Biochemistry 54</i>, 3129–3132], and both reactions likely proceed by the same mechanism. In the MJ0100-catalyzed reaction, Rauch has proposed [Rauch, B. L. (2017) <i>Biochemistry 56</i>, 1051–1061] that MJ1526 and its homologues in other methanogens likely supply the sulfane sulfur required for the reaction. Enzyme Catalyzing;Methanogens Coenzyme M;coenzyme M;Communication reports;MJ 0099 proteins;biosynthesi;Biochemistry;identification;sulfane sulfur;Rauch;enzyme catalyzing;methanogen;thiol group;coenzyme M synthase;2- mercaptoethanesulfonic acid;MJ 1526;MJ 0100-catalyzed reaction;MJ 0100 2019-04-01
    https://acs.figshare.com/articles/journal_contribution/Identification_of_an_Enzyme_Catalyzing_the_Conversion_of_Sulfoacetaldehyde_to_2_Mercaptoethanesulfonic_Acid_in_Methanogens/7960712
10.1021/acs.biochem.9b00176.s001