Книга: Diana Shem «Catalysis of Orotidine 5 -Monophosphate»
|
Производитель: "LAP Lambert Academic Publishing" As a model for interactions present in the active site of orotidine-5 -monophosphate decarboxylase (ODCase), we investigated the effects of substrate destabilization by a nearby negative charge and stabilization of the carbanion intermediate, due to hydrogen bonds to the carbonyl groups (O-2 and O-4) of orotic acid and its decarboxylation product, using ab initio calculations. Results from these models were comparable with available data, suggesting that the magnitude of the decarboxylation rate enhancement depends on a combination of the charge distance and hydrogen bonding effects. We found that the dipole moment of the proton donor may also play a significant role, implying that the key to the rest of the catalysis lie within the specific interactions of the substrate and the surrounding residues. ISBN:9783844380880 Издательство: "LAP Lambert Academic Publishing" (2011)
ISBN: 9783844380880 |
См. также в других словарях:
Orotidine 5'-phosphate decarboxylase — E. coli OMP decarboxylase.[1] Identifiers EC number … Wikipedia
Enzyme — Biocatalyst redirects here. For the use of natural catalysts in organic chemistry, see Biocatalysis. Human glyoxalase I. Two zinc ions that are needed for the enzyme to catalyze its reaction are shown as purp … Wikipedia
Metabolism — Cell metabolism redirects here. For the journal, see Cell Metabolism. Structure of adenosine triphosphate, a central intermediate in energy metabolism Metabolism (from Greek: μεταβολή metabolē , change or Greek: μεταβολισμός metabolismos,… … Wikipedia
Phosphoenolpyruvate carboxykinase — Not to be confused with Phosphoenolpyruvate carboxylase. Phosphoenolpyruvate carboxykinase PDB rendering based on 1khb. Identifiers Symbol … Wikipedia
Dihydrofolate reductase — Ribbon diagram of human dihydrofolate reductase in complex with folate (blue). From PDB 1DRF … Wikipedia
