Ontology highlight
ABSTRACT:
SUBMITTER: Mehta AP
PROVIDER: S-EPMC4227724 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20140718 30
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 pr ...[more]