Open AccessBioconversion of pyrimidine by resting cells of quinoline‐degrading bacteria
Author(s) -
Fetzner Susanne
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13675.x
Subject(s) - comamonas testosteroni , quinoline , pyrimidine , uracil , chemistry , comamonas , substrate (aquarium) , biochemistry , bacteria , stereochemistry , enzyme , organic chemistry , biology , pseudomonas , dna , ecology , genetics
Nine quinoline‐degrading bacterial strains were tested for their ability to hydroxylate pyrimidine. All strains converted pyrimidine to uracil via pyrimidine‐4‐one in a cometabolic process. Quinoline 2‐oxidoreductases (QuinORs) were the catalysts of fortuitous pyrimidine hydroxylation. Whereas in most strains the activity of the QuinOR towards pyrimidine was very low compared to its activity towards quinoline, QuinOR in crude extracts from Comamonas testosteroni 63 showed a specific activity of 64 (mU mg protein) −1 with pyrimidine as substrate, compared to a specific activity of 237 (mU mg protein) −1 towards the intrinsic substrate quinoline. Resting cells of Comamonas testosteroni 63 rapidly converted pyrimidine almost stoichiometrically to uracil, which accumulated in the cell suspension. Using an adsorbent resin, uracil was prepared from the supernatant of Comamonas testosteroni 63 resting cells with a yield of >98%.