Lessons From the Studies of a CC Bond Forming Radical SAM Enzyme in Molybdenum Cofactor Biosynthesis.

ABSTRACT: MoaA is one of the founding members of the radical S-adenosyl-_L-methionine (SAM) superfamily, and together with the second enzyme, MoaC, catalyzes the construction of the pyranopterin backbone structure of the molybdenum cofactor (Moco). However, the exact functions of both MoaA and MoaC had remained ambiguous for more than 2 decades. Recently, their functions were finally elucidated through successful characterization of the MoaA product as 3',8-cyclo-7,8-dihydro-GTP (3',8-cH₂GTP), which was shown to be converted to cyclic pyranopterin monophosphate (cPMP) by MoaC. 3',8-cH₂GTP was produced in a small quantity and was highly oxygen sensitive, which explains why this compound had previously eluded characterization. This chapter describes the methodologies fo

SUBMITTER: Pang H 

PROVIDER: S-EPMC6263026 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature