The structural basis for the remarkable catalytic proficiency of orotidine 5′-monophosphate decarboxylase
Open Access
- 6 December 2000
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 10 (6) , 711-718
- https://doi.org/10.1016/s0959-440x(00)00148-2
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- 13C Kinetic Isotope Effects and the Mechanism of the Uncatalyzed Decarboxylation of Orotic AcidJournal of the American Chemical Society, 2000
- Electrostatic stress in catalysis: Structure and mechanism of the enzyme orotidine monophosphate decarboxylaseProceedings of the National Academy of Sciences, 2000
- The crystal structure and mechanism of orotidine 5′-monophosphate decarboxylaseProceedings of the National Academy of Sciences, 2000
- The Mechanism of Orotidine 5‘-Monophosphate Decarboxylase: Catalysis by Destabilization of the SubstrateBiochemistry, 2000
- Mechanism of decarboxylation of 1,3-dimethylorotic acid revisited: Trapping of the reaction intermediateTetrahedron Letters, 1998
- Short, Strong Hydrogen Bonds in the Gas Phase and in Solution: Theoretical Exploration of pKa Matching and Environmental Effects on the Strengths of Hydrogen Bonds and Their Potential Roles in Enzymatic CatalysisThe Journal of Organic Chemistry, 1998
- A Proficient Enzyme Revisited: The Predicted Mechanism for Orotidine Monophosphate DecarboxylaseScience, 1997
- A Proficient EnzymeScience, 1995
- Model chemistry for a covalent mechanism of action of orotidine 5'-phosphate decarboxylaseJournal of the American Chemical Society, 1982
- Mechanism of decarboxylation of 1,3-dimethylorotic acid. A model for orotidine 5'-phosphate decarboxylaseJournal of the American Chemical Society, 1976