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

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

• Begley, Tadhg

published proceedings

• J Am Chem Soc

altmetric score

• 3

author list (cited authors)

• Bhandari, D. M., Fedoseyenko, D., & Begley, T. P.

citation count

• 36

complete list of authors

• Bhandari, Dhananjay M||Fedoseyenko, Dmytro||Begley, Tadhg P

publication date

• December 2016

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Biocatalysis
• Catalytic Domain
• Free Radicals
• Lyases
• Models, Molecular
• S-adenosylmethionine
• Tryptophan

PubMed Central ID

• 27998091

Digital Object Identifier (DOI)

• 10.1021/jacs.6b06139

start page

• 16184

end page

• 16187

volume

• 138

issue

• 50

URL

• http://dx.doi.org/10.1021/jacs.6b06139