当前位置: X-MOL 学术J. Am. Chem. Soc. › 论文详情
Mechanistic Studies on Tryptophan Lyase (NosL): Identification of Cyanide as a Reaction Product
Journal of the American Chemical Society ( IF 13.858 ) Pub Date : 2018-01-02 , DOI: 10.1021/jacs.7b09000
Dhananjay M. Bhandari, Dmytro Fedoseyenko, Tadhg P. Begley

Tryptophan lyase (NosL) catalyzes the formation of 3-methylindole-2-carboxylic acid and 3-methylindole from l-tryptophan. In this paper, we provide evidence supporting a formate radical intermediate and demonstrate that cyanide is a byproduct of the NosL-catalyzed reaction with l-tryptophan. These experiments require a major revision of the NosL mechanism and uncover an unanticipated connection between NosL and HydG, the radical SAM enzyme that forms cyanide and carbon monoxide from tyrosine during the biosynthesis of the metallo-cluster of the [Fe–Fe] hydrogenase.
更新日期:2018-01-03

 

Some contents have been Reproduced with permission of the American Chemical Society.
Some contents have been Reproduced by permission of The Royal Society of Chemistry.
分享到
评论: 0
期刊列表
Wiley论文编辑服务,每月大奖送不停!
南京大学化学化工学院谢劲课题组招聘启事
广州大学水污染过程与控制研究团队招聘启事
华中师范大学第一届国际青年学者化学科学论坛
【问答】谍反应有哪些重要应用?
X-MOL近期新增451种期刊(20171216)
2017年中科院JCR分区化学大类列表
试剂库存管理
化合物查询
down
wechat
bug