OMP decarboxylase—An enigma persists
- 1 December 2007
- journal article
- review article
- Published by Elsevier in Bioorganic Chemistry
- Vol. 35 (6) , 465-469
- https://doi.org/10.1016/j.bioorg.2007.07.004
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Activation of Orotidine 5‘-Monophosphate Decarboxylase by Phosphite Dianion: The Whole Substrate is the Sum of Two PartsJournal of the American Chemical Society, 2005
- The effective molarity of the substrate phosphoryl group in the transition state for yeast OMP decarboxylaseBioorganic Chemistry, 2005
- Catalytic Proficiency: The Unusual Case of OMP DecarboxylaseAnnual Review of Biochemistry, 2002
- Dissecting a Charged Network at the Active Site of Orotidine-5′-phosphate DecarboxylaseJournal of Biological Chemistry, 2001
- Structural Basis for the Catalytic Mechanism of a Proficient Enzyme: Orotidine 5‘-Monophosphate Decarboxylase,Biochemistry, 2000
- Anatomy of a proficient enzyme: The structure of orotidine 5′-monophosphate decarboxylase in the presence and absence of a potential transition state analogProceedings of the National Academy of Sciences, 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
- No Metal Cofactor in Orotidine 5′-Monophosphate DecarboxylaseBiochemical and Biophysical Research Communications, 1999
- A Proficient EnzymeScience, 1995