Pseudomonas fluorescensStrain R124 Encodes Three Different MIO Enzymes

• DOI: 10.1002/cbic.201700530
• Publication Date: 2017-11-29T16:35:29Z
• Authors: Pál Csuka; Vivien Juhász; Szabolcs Kohári; Alina Filip; Andrea Varga; Péter Sátorhelyi; László Csaba Bencze; Hazel Barton; Csaba Paizs; László Poppe
• Keywords: Pseudomonas fluorescens; Biocatalysis; Lyase; Phenylalanine ammonia-lyase

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