Hydrogen isotope tracing in the reaction of orotidine-5′-monophosphate decarboxylase
✍ Scribed by Jeffrey A Smiley; Brian J DelFraino; Beth A Simpson
- Book ID
- 117042475
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 183 KB
- Volume
- 412
- Category
- Article
- ISSN
- 0003-9861
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📜 SIMILAR VOLUMES
Human UMP synthase is a bifunctional enzyme that catalyzes the penultimate and last steps in the de novo biosynthesis of UMP. In contrast to prokaryotes, UMP synthase from higher eukaryotes combines the orotate phosphoribosyltransferase and the orotidine-5'-monophosphate (OMP) decarboxylase activiti
A potential alternate substrate for orotidine-5Ј-monophosphate decarboxylase, 2-thio-orotidine-5Ј-monophosphate, was synthesized enzymatically and purified by a modification of a previous account (K. Shostak, and M. E. Jones 1992, Biochemistry 31, 12155-12161). Characterization of the product was co