Tryptophan Lyase (NosL): A Cornucopia of 5′-Deoxyadenosyl Radical Mediated Transformations

被引：43

作者：

Bhandari, Dhananjay M. ^{[1
]}

Fedoseyenko, Dmytro ^{[1
]}

Begley, Tadhg P. ^{[1
]}

机构：

[1] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2016年 / 138卷 / 50期

关键词：

METHIONINE ENZYME NOSL; MECHANISTIC INSIGHTS; BIOTIN SYNTHASE; SAM ENZYMES; BIOSYNTHESIS; CATALYSIS; MENAQUINONE; MUTAGENESIS; INSERTION; REQUIRES;

D O I：

10.1021/jacs.6b06139

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

Tryptophan lyase (NosL) is a radical S-adenosyl-L-methionine (SAM) enzyme that catalyzes the formation of 3-methyl-2-indolic acid from L-tryptophan. In this paper, we demonstrate that the S'-deoxyadenosyl radical is considerably more versatile in its chemistry than previously anticipated: hydrogen atom abstraction from N-alpha-cydopropyltryptophan occurs at C alpha rather than the amino group with NosL Y90A and replacing the substrate amine with a ketone or an alkene changes the chemistry from hydrogen atom abstraction to double bond addition. In addition, the 5'-deoxyadenosyl radical can add to the [4Fe-4S] cluster and dithionite can be used to trap radicals at the active site.

引用

页码：16184 / 16187

页数：4

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