Title
A two-component protease in Methylorubrum extorquens with high activit toward the peptide precursor of the redox cofactor pyrroloquinoline quinone
Digital Object Identifier / DOI
https://doi.org/10.1074/jbc.ra119.009684
Department
Natural Sciences and Mathematics
Document Type
Article
Source
Journal of Biochemistry
Publication Date
10-11-2019
ISSN
1083-351X
Volume
294
Issue
41
First Page
15025
Last Page
15036
Abstract
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
PubMed ID
31427437
Rights
© 2019 Martins et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.