Format

Send to

Choose Destination
Chembiochem. 2018 Feb 16;19(4):411-418. doi: 10.1002/cbic.201700530. Epub 2018 Jan 4.

Pseudomonas fluorescens Strain R124 Encodes Three Different MIO Enzymes.

Author information

1
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, 1111, Budapest, Hungary.
2
Fermentia Microbiological Ltd, Berlini út 47-49, 1049, Budapest, Hungary.
3
Biocatalysis and Biotransformation Research Center, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János str. 11, 400028, Cluj-Napoca, Romania.
4
Department of Biology, The University of Akron, ASEC West Tower 178, Akron, OH, 44325, USA.
5
SynBiocat Ltd, Szilasliget u. 3, 1172, Budapest, Hungary.

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.

KEYWORDS:

biocatalysis; gene transfer; lyases; nitrogen; phenylalanine

PMID:
29193598
DOI:
10.1002/cbic.201700530

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center