A two-component protease in Methylorubrum extorquens with high activit toward the peptide precursor of the redox cofactor pyrroloquinoline quinone

Authors

Ana M. Martins, California Institute for Quantitative Biosciences, University of California, Berkeley
John A. Latham, Department of Chemistry and Biochemistry, University of DenverFollow
Paulo J. Martel, Centre for Biomedical Research, University of the Algarve
Ian Barr, California Institute for Quantitative Biosciences, University of California, BerkeleyFollow
Anthony T. Iavarone, California Institute for Quantitative Biosciences, University of California, Berkeley
Judith P. Klinman, California Institute for Quantitative Biosciences, University of California, BerkeleyFollow

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.