Abstract：
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.
摘要：
许多放线菌包含铁依赖性酶的结构基因，这些铁依赖性酶通过O2依赖性双氧合消耗麦角硫因。所得产物麦角硫因亚磺酸在生理条件下是稳定的,除非通过专用脱硫酶催化裂解成二氧化硫和三甲基组氨酸。该报告记录了两种类型的麦角硫因亚磺脱硫酶通过趋同进化而进化。一种类型与金属依赖性脱羧酶有关，而另一种类型则属于类罗丹酶的超家族。成对的麦角硫因双加氧酶（ETDO）和麦角硫因亚硫酸脱硫酶（ETSD）出现在数千个测序的放线菌中，表明氧化麦角硫因降解是该门的常见活性。
