Molybdopterin biosynthesis: trapping an unusual purine ribose adduct in the MoaA-catalyzed reaction. Academic Article

abstract

• MoaA/MoaC catalyze a remarkable rearrangement reaction in which guanosine-5'-triphosphate (GTP) is converted to cyclic pyranopterin monophosphate (cPMP). In this reaction, the C8 of GTP is inserted between the C2' and the C3' carbons of the GTP ribose. Previous experiments with GTP isotopomers demonstrated that the ribose C3' hydrogen atom is abstracted by the adenosyl radical. This led to a novel mechanistic proposal involving an intermediate with a bond between the C8 of guanine and C3' of the ribose. This paper describes the use of 2',3'-dideoxyGTP to trap this intermediate.

authors

• Begley, Tadhg

published proceedings

• J Am Chem Soc

altmetric score

• 0.25

author list (cited authors)

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

citation count

• 25

complete list of authors

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

publication date

• July 2013

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Biocatalysis
• Coenzymes
• Guanosine Triphosphate
• Hydrolases
• Metalloproteins
• Pteridines
• Ribose

PubMed Central ID

• 23848839

Digital Object Identifier (DOI)

• 10.1021/ja4041048

start page

• 10883

end page

• 10885

volume

• 135

issue

• 30

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja4041048