Identification of an Enzyme Catalyzing the Conversion of Sulfoacetaldehyde to 2-Mercaptoethanesulfonic Acid in Methanogens.

Abstract

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) Biochemistry 54, 3129-3132], and both reactions likely proceed by the same mechanism. In the MJ0100-catalyzed reaction, Rauch has proposed [Rauch, B. L. (2017) Biochemistry 56, 1051-1061] that MJ1526 and its homologues in other methanogens likely supply the sulfane sulfur required for the reaction.