Tryptophan Lyase (NosL): A Cornucopia of 5′-Deoxyadenosyl Radical Mediated Transformations | Academic Article individual record
abstract

© 2016 American Chemical Society. 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 N α -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.

authors
author list (cited authors)
Bhandari, D. M., Fedoseyenko, D., & Begley, T. P.
publication date
2016
keywords
  • Free Radicals
  • Lyases
  • S-adenosylmethionine
  • Catalytic Domain
  • Tryptophan
  • Biocatalysis
  • Models, Molecular
citation count

21