Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4
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 hydr...
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| Format: | Article |
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Oxford University Press
1995
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| Online Access: | http://psasir.upm.edu.my/id/eprint/116518/ |
| _version_ | 1848867023434547200 |
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| author | Ogawa, Jun Honda, Michinari Shimizu, Sakayu Soong, Chee Leong |
| author_facet | Ogawa, Jun Honda, Michinari Shimizu, Sakayu Soong, Chee Leong |
| author_sort | Ogawa, Jun |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T14:29:54Z |
| format | Article |
| id | upm-116518 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:29:54Z |
| publishDate | 1995 |
| publisher | Oxford University Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1165182025-04-10T00:59:27Z http://psasir.upm.edu.my/id/eprint/116518/ Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 Ogawa, Jun Honda, Michinari Shimizu, Sakayu Soong, Chee Leong 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. Oxford University Press 1995 Article PeerReviewed 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 https://academic.oup.com/bbb/article/59/10/1960-1962/5951756 10.1271/bbb.59.1960 |
| spellingShingle | Ogawa, Jun Honda, Michinari Shimizu, Sakayu Soong, Chee Leong Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 |
| title | Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 |
| title_full | Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 |
| title_fullStr | Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 |
| title_full_unstemmed | Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 |
| title_short | Diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in Blastobacter sp. A17P-4 |
| title_sort | diversity of cyclic ureide compound-, dihydropyrimidine-, and hydantoin-hydrolyzing enzymes in blastobacter sp. a17p-4 |
| url | http://psasir.upm.edu.my/id/eprint/116518/ http://psasir.upm.edu.my/id/eprint/116518/ http://psasir.upm.edu.my/id/eprint/116518/ |