Pseudomonas fluorescens Strain R124 Encodes Three Different MIO Enzymes

Pál Csuka, Vivien Juhász, Szabolcs Kohári, Alina Filip, Andrea Varga, Péter Sátorhelyi, László Csaba Bencze, Hazel Barton, Csaba Paizs, L. Poppe

Research output: Article

5 Citations (Scopus)

Abstract

A number of class I lyase-like enzymes, including aromatic ammonia-lyases and aromatic 2,3-aminomutases, contain the electrophilic 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) catalytic moiety. This study reveals that Pseudomonas fluorescens R124 strain isolated from a nutrient-limited cave encodes a histidine ammonia-lyase, a tyrosine/phenylalanine/histidine ammonia-lyase (XAL), and a phenylalanine 2,3-aminomutase (PAM), and demonstrates that an organism under nitrogen-limited conditions can develop novel nitrogen fixation and transformation pathways to enrich the possibility of nitrogen metabolism by gaining a PAM through horizontal gene transfer. The novel MIO enzymes are potential biocatalysts in the synthesis of enantiopure unnatural amino acids. The broad substrate acceptance and high thermal stability of PfXAL indicate that this enzyme is highly suitable for biocatalysis.

Original languageEnglish
Pages (from-to)411-418
Number of pages8
JournalChemBioChem
Volume19
Issue number4
DOIs
Publication statusPublished - febr. 16 2018

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

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    Csuka, P., Juhász, V., Kohári, S., Filip, A., Varga, A., Sátorhelyi, P., Bencze, L. C., Barton, H., Paizs, C., & Poppe, L. (2018). Pseudomonas fluorescens Strain R124 Encodes Three Different MIO Enzymes. ChemBioChem, 19(4), 411-418. https://doi.org/10.1002/cbic.201700530