Citation
Ogawa, Jun and Honda, Michinari and Shimizu, Sakayu and Soong, Chee Leong
(1995)
Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4.
Bioscience, Biotechnology, and Biochemistry, 59 (10).
pp. 1960-1962.
ISSN 0916-8451; eISSN: 1347-6947
Abstract
Two cyclic ureide compound-hydrolyzing enzymes were found in Blastobacter sp. A17p-4, and partially purified. One hydrolyzed 5-substituted hydantoins D-stereospecifically and had dihydropyrimidinase activity. The other was a novel enzyme which should be called an imidase. The imidase preferably hydrolyzed cyclic imide compounds such as glutarimide and succinimide more than cyclic ureide compounds, and produced monoamidated dicarboxylates. © 1995, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
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Additional Metadata
| Item Type: | Article |
|---|---|
| Divisions: | Faculty of Science and Environmental Studies |
| DOI Number: | https://doi.org/10.1271/bbb.59.1960 |
| Publisher: | Oxford University Press |
| Keywords: | Blastobacter sp. A17P-4; Cyclic ureide compounds; Dihydropyrimidinase; Hydantoinase; Imidase; Enzyme diversity; Glutarimide; Succinimide; 5-substituted hydantoins; D-stereospecific hydrolysis; Monoamidated dicarboxylates |
| Depositing User: | Ms. Azian Edawati Zakaria |
| Date Deposited: | 10 Apr 2025 00:59 |
| Last Modified: | 10 Apr 2025 00:59 |
| Altmetrics: | http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1271/bbb.59.1960 |
| URI: | http://psasir.upm.edu.my/id/eprint/116518 |
| Statistic Details: | View Download Statistic |
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