Tryptophan Lyase (NosL): A Cornucopia of 5'-Deoxyadenosyl Radical Mediated Transformations.
|
Academic Article
individual record
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 N-cyclopropyltryptophan occurs at C 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
publication outlet
J Am Chem Soc
author list (cited authors)
Bhandari, D. M., Fedoseyenko, D., & Begley, T. P.
publication date
2016
publisher
American Chemical Society (ACS)
Publisher
keywords
- Free Radicals
- Lyases
- S-adenosylmethionine
- Catalytic Domain
- Tryptophan
- Biocatalysis
- Models, Molecular
altmetric score
3.0
citation count
36
PubMed ID
27998091
identifier
290378SE
Digital Object Identifier (DOI)
start page
16184
end page
16187
volume
138
issue
50