Global ETD Search

Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.

Results

Showing 1 to 4 of 4 for “"Orotidine 5'-monophosphate decarboxylase (OMPDC)"”.

  1. 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 …

    uiuc Repository record for Investigations into the mechanism of orotidine 5'-monophosphate decarboxylase: Sources of substrate destabilization and transition state stabilization (opens in a new tab)

  2. 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 …

    uiuc Repository record for Evolution of Enzymatic Activities in the OMPDC Suprafamily: Discovery, Design and Evolution of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase (opens in a new tab)

  3. 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 …

    uiuc Repository record for Structural requirements for enzymatic efficiency in cofactor-independent decarboxylation (opens in a new tab)

  4. 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 …

    uiuc Repository record for In search of catalytic proficiency: The importance of enzyme conformational change to orotidine 5’-monophosphate decarboxylase catalysis (opens in a new tab)