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...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Published: |
Oxford University Press
1995
|
| Online Access: | http://psasir.upm.edu.my/id/eprint/116518/ |
| Summary: | 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. |
|---|