Open AccessEvaluation of pyrimidine‐ and hydantoin‐degrading enzyme activities in aerobic bacteria
Author(s) -
Ogawa Jun,
Kaimura Takeshi,
Yamada Hideaki,
Shimizu Sakayu
Publication year - 1994
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.1574-6968.1994.tb07143.x
Subject(s) - hydantoin , pyrimidine , enzyme , pseudomonas putida , amidohydrolase , pyrimidine metabolism , stereochemistry , bacteria , biochemistry , chemistry , amidase , amide , stereospecificity , biology , purine , catalysis , genetics
The enzyme activities responsible for the reductive pyrimidine base degradation by aerobic bacteria, which produce hydantoin‐degrading enzymes, were investigated. Pseudomonas putida IFO 12996, which is a d‐stereospecific hydantoinase producer, has dihydropyrimidinase activity, and Comamonas sp. E222c and Blastobacter sp. A17p‐4, which are N‐carbamoyl‐D‐amino acid amidohydrolase producers, have β‐ureidopropionase activity. Blastobacter sp. also possesses both d‐stereospecific hydantoinase and dihydropyrimidinase activities. Thus, two amide ring‐opening activities and/or two N ‐carbamoyl amino acid‐hydrolyzing activities coexist in these bacteria. However, the differences of the induction levels of each enzyme activities for the several pyrimidine‐ and hydantoin‐related compounds suggest that these corresponding amide ring‐opening or N ‐carbamoyl amino acid‐hydrolyzing activities are not always catalyzed by the same enzymes.