Tryptophan Lyase (NosL): A Cornucopia of 5'-Deoxyadenosyl Radical Mediated Transformations - PubMed (original) (raw)

. 2016 Dec 21;138(50):16184-16187.

doi: 10.1021/jacs.6b06139. Epub 2016 Dec 8.

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

Dhananjay M Bhandari et al. J Am Chem Soc. 2016.

Abstract

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 5'-deoxyadenosyl radical is considerably more versatile in its chemistry than previously anticipated: hydrogen atom abstraction from Nα-cyclopropyltryptophan occurs at Cα 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.

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