Molybdopterin biosynthesis: trapping of intermediates for the MoaA-catalyzed reaction using 2'-deoxyGTP and 2'-chloroGTP as substrate analogues. Academic Article

abstract

• MoaA is a radical S-adenosylmethionine (AdoMet) enzyme that catalyzes a complex rearrangement of guanosine-5'-triphosphate (GTP) in the first step of molybdopterin biosynthesis. In this paper, we provide additional characterization of the MoaA reaction product, describe the use of 2'-chloroGTP to trap the GTP C3' radical, generated by hydrogen atom transfer to the 5'-deoxyadenosyl radical, and the use of 2'-deoxyGTP to block a late step in the reaction sequence. These probes, coupled with the previously reported trapping of an intermediate in which C3' of the ribose is linked to C8 of the purine, allow us to propose a plausible mechanism for the MoaA-catalyzed reaction.

authors

• Begley, Tadhg

published proceedings

• J Am Chem Soc

author list (cited authors)

• Mehta, A. P., Abdelwahed, S. H., Xu, H., & Begley, T. P.

citation count

• 18

complete list of authors

• Mehta, Angad P||Abdelwahed, Sameh H||Xu, Hui||Begley, Tadhg P

publication date

• July 2014

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Coenzymes
• Escherichia Coli
• Escherichia Coli Proteins
• Guanosine Triphosphate
• Halogenation
• Isomerases
• Metalloproteins
• Pteridines
• Substrate Specificity

PubMed Central ID

• 24955657

Digital Object Identifier (DOI)

• 10.1021/ja502663k

start page

• 10609

end page

• 10614

volume

• 136

issue

• 30

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja502663k