Abstract
Kinetic analysis of decarboxylation catalyzed by S154A, Q215A, and S154A/Q215A mutant yeast orotidine 5′-monophosphate decarboxylases with orotidine 5′-monophosphate (OMP) and with a truncated nucleoside substrate (EO) activated by phosphite dianion shows (1) the side chain of Ser-154 stabilizes the transition state through interactions with the pyrimidine rings of OMP or EO, (2) the side chain of Gln-215 interacts with the phosphodianion group of OMP or with phosphite dianion, and (3) the interloop hydrogen bond between the side chains of Ser-154 and Gln-215 orients the amide side chain of Gln-215 to interact with the phosphodianion group of OMP or with phosphite dianion.
Original language | English (US) |
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Pages (from-to) | 7785-7787 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 47 |
Issue number | 30 |
DOIs | |
State | Published - Jul 29 2008 |
ASJC Scopus subject areas
- Biochemistry