Characterization of auxiliary iron-sulfur clusters in a radical S-adenosylmethionine enzyme PqqE from Methylobacterium extorquens AM1.

ABSTRACT: PqqE is a radical S-adenosyl-l-methionine (SAM) enzyme that catalyzes the initial reaction of pyrroloquinoline quinone (PQQ) biosynthesis. PqqE belongs to the SPASM (subtilosin/PQQ/anaerobic sulfatase/mycofactocin maturating enzymes) subfamily of the radical SAM superfamily and contains multiple Fe-S clusters. To characterize the Fe-S clusters in PqqE from Methylobacterium extorquens AM1, Cys residues conserved in the N-terminal signature motif (CX ₃ CX ₂C) and the C-terminal seven-cysteine motif (CX _9-15 GX ₄ CX _n CX ₂ CX ₅ CX ₃ CX _n C; n = an unspecified number) were individually or simultaneously mutated into Ser. Biochemical and Mössbauer s

SUBMITTER: Saichana N 

PROVIDER: S-EPMC5715301 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature