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Showing 1 to 6 of 6 for “"Orotidine 5'-monophosphate decarboxylase"”.
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In Search of Catalytic Proficiency: The Importance of Enzyme Conformational Change to Orotidine 5'-Monophosphate Decarboxylase Catalysis
By applying the tools of enzymology learned in the Gerlt Laboratory and working successfully with numerous collaborators, I have furthered our understanding of the mechanism of one of Nature's best catalysts, OMPDC. Increasingly in enzymology, the role of conformational change in enzyme catalysis …
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In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5’-monophosphate decarboxylase catalysis
… a TIM-barrel enzyme in pyrimidine biosynthesis, orotidine 5’-monophosphate decarboxylase (OMPDC). OMPDC catalyzes the decarboxylation of OMP to UMP; the uncatalyzed rate for this reaction has been estimated to be 2.8 x 1016 s-1 (1). The slow rate without OMPDC is attributable to the lack of …
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Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization
Orotidine 5′-monophosphate decarboxylase (OMPDC) achieves a rarely paralleled rate acceleration, yet the catalytic basis prompting this enhancement have yet to be fully elucidated. To accomplish decarboxylation, OMPDC must overcome the high energy barrier due to the localized anionic charge of the …
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Evolution of Enzymatic Activities in the OMPDC Suprafamily: Discovery, Design and Evolution of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) was discovered to be involved in the fermentative utilization of L-ascorbate by enteric bacteria such as E. coli K-12. KGPDC is a new member of the orotidine 5'-monophosphate decarboxylase (OMPDC) suprafamily, and its discovery expands the range …
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Investigation of Substrate Specificity in Phosphate Binding Barrels and Mechanistic Studies of Orotidine Monophosphate Decarboxylase
"Orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum (MtOMPDC) catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) and uridine 5'-monophosphate (UMP) with an enormous rate acceleration, 1.8 x 1016 (kcat = 5 s-1, 25°C; knon = 2.8 x 1016 s-1), and …
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Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation
Orotidine 5’-monophosphate decarboxylase (OMPDC) is the last enzyme in the de novo pyrimidine biosynthetic pathway. It catalyzes the decarboxylation of orotidine 5’-monophosphate (OMP) to uridine 5’-monophosphate (UMP), without the requirement of a cofactor. It provides catalytic rate enhancements …