A two-component protease in Methylorubrum extorquens with high activit toward the peptide precursor of the redox cofactor pyrroloquinoline quinone
Digital Object Identifier / DOI
Natural Sciences and Mathematics
Journal of Biochemistry
Pyrroloquinoline quinone is a prominent redox cofactor in many prokaryotes, produced from a ribosomally synthesized and post-translationally modified peptide PqqA via a pathway comprising four conserved proteins PqqB-E. These four proteins are now fairly well-characterized and span radical SAM activity (PqqE), aided by a peptide chaperone (PqqD), a dual hydroxylase (PqqB), and an eight-electron, eight-proton oxidase (PqqC). A full description of this pathway has been hampered by a lack of information regarding a protease/peptidase required for the excision of an early, cross-linked di-amino acid precursor to pyrroloquinoline quinone. Herein, we isolated and characterized a two-component heterodimer protein from the α-proteobacterium
© 2019 Martins et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.