Catalysis of a new ribose carbon-insertion reaction by the molybdenum cofactor biosynthetic enzyme MoaA

Angad P. Mehta, Jeremiah W. Hanes, Sameh H. Abdelwahed, David G. Hilmey, Petra Hänzelmann, Tadhg P. Begley

Research output: Contribution to journalArticlepeer-review

Abstract

MoaA, a radical S-adenosylmethionine enzyme, catalyzes the first step in molybdopterin biosynthesis. This reaction involves a complex rearrangement in which C8 of guanosine triphosphate is inserted between C2′ and C3′ of the ribose. This study identifies the site of initial hydrogen atom abstraction by the adenosyl radical and advances a mechanistic proposal for this unprecedented reaction.

Original languageEnglish (US)
Pages (from-to)1134-1136
Number of pages3
JournalBiochemistry
Volume52
Issue number7
DOIs
StatePublished - Feb 19 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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