Biochemical properties of CumA multicopper oxidase from plant pathogen, Pseudomonas syringae

Konan Ishida, Yuya Tsukamoto, Masaki Horitani, Tomohisa Ogawa, Yoshikazu Tanaka

Research output: Contribution to journalArticlepeer-review

Abstract

Multicopper oxidases have a wide range of substrate specificity to be involved in various physiological reactions. Pseudomonas syringae, a plant pathogenic bacterium, has a multicopper oxidase, CumA. Multicopper oxidases have ability to degrade plant cell wall component, lignin. Once P. syringae enter apoplast and colonize, they start to disrupt plant immunity. Therefore, deeper understanding of multicopper oxidases from plant pathogens helps to invent measures to prevent invasion into plant cell, which brings agricultural benefits. Several biochemical studies have reported lower activity of CumA compared with other multicopper oxidase called CotA. However, the mechanisms underlying the difference in activity have not yet been revealed. In order to acquire insight into them, we conducted a biophysical characterization of PsCumA. Our results show that PsCumA has weak type I copper EPR signal, which is essential for oxidation activity. We propose that difference in the coordination of copper ions may decrease reaction frequency.

Original languageEnglish
Pages (from-to)1995-2002
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume85
Issue number9
DOIs
Publication statusPublished - 2021 Sep 1

Keywords

  • CotA
  • CumA
  • multicopper oxidase
  • Pseudomonas syringae

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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