%0 Journal Article
%T A Rhodanese-Like Enzyme that Catalyzes Desulfination of Ergothioneine Sulfinic Acid.
%A Nalivaiko EY
%A Seebeck FP
%J Chembiochem
%V 25
%N 9
%D 2024 May 2
%M 38597743
%F 3.461
%R 10.1002/cbic.202400131
%X Many actinobacterial species contain structural genes for iron-dependent enzymes that consume ergothioneine by way of O2-dependent dioxygenation. The resulting product ergothioneine sulfinic acid is stable under physiological conditions unless cleavage to sulfur dioxide and trimethyl histidine is catalyzed by a dedicated desulfinase. This report documents that two types of ergothioneine sulfinic desulfinases have evolved by convergent evolution. One type is related to metal-dependent decarboxylases while the other belongs to the superfamily of rhodanese-like enzymes. Pairs of ergothioneine dioxygenases (ETDO) and ergothioneine sulfinic acid desulfinase (ETSD) occur in thousands of sequenced actinobacteria, suggesting that oxidative ergothioneine degradation is a common activity in this phylum.