期刊
ACS CATALYSIS
卷 13, 期 23, 页码 15417-15426出版社
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.3c04026
关键词
nonheme iron enzyme; ovothiol; ergothioneine; X-ray structure; regioselectivity; sulfur-containingnatural products
This study successfully obtained the crystal structure of OvoA and provided critical information about its C-S bond formation regioselectivity. Additionally, it revealed that OvoA exhibits multiple additional activities, paving the way for future studies on structure-function correlations.
Ovothiol A and ergothioneine are thiol-histidine derivatives with sulfur substitutions at the delta-carbon or epsilon-carbon of the l-histidine imidazole ring, respectively. Both ovothiol A and ergothioneine have protective effects on many aging-related diseases, and the sulfur substitution plays a key role in determining their chemical and biological properties, while factors governing sulfur incorporation regioselectivities in ovothiol and ergothioneine biosynthesis in the corresponding enzymes (OvoA, Egt1, or EgtB) are not yet known. In this study, we have successfully obtained the first OvoA crystal structure, which provides critical information to explain their C-S bond formation regioselectivity. Furthermore, OvoA(Th2) exhibits several additional activities: (1) ergothioneine sulfoxide synthase activity akin to Egt1 in ergothioneine biosynthesis; (2) cysteine dioxygenase activity using l-cysteine and l-histidine analogues as substrates; (3) cysteine dioxygenase activity upon mutation of an active site tyrosine residue (Y406). The structural insights and diverse chemistries demonstrated by OvoA(Th2) pave the way for future comprehensive structure-function correlation studies.
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