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.

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