Sandbox Reserved 315: Difference between revisions
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=Introduction= | =Introduction= | ||
'''Orotidine monophosphate decarboxylase''' (ODCase), also known as '''orotidine 5’-monophosphate decarboxylase''' (OMP decarboxylase) or '''orotidine 5’-phosphate decarboxylase''' is an enzyme involved in pyrimidine biosynthesis. It catalyzes the conversion of orotidine 5’-monophosphate (OMP) to uridine 5’-monophosphate (UMP). This reaction is the final step in de novo pyrimidine nucleotide synthesis and is an essential precursor for both DNA and RNA. The main structure of orotidine monophosphate decarboxylase is a TIM barrel, with one side acting as the binding site, while the other side is closed-off. This enzyme has been studied for it’s extreme catalytic proficiency<Ref name = "Miller">PMID:10681417</ref>. | |||
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=== | =Protein Structure= | ||
= | ==TIM Barrel== | ||
==Active Site== | |||
=Rate of Catalysis= | |||
==Substrate Destabilization== | |||
<Ref name = "Lee">PMID:9139656</ref> | |||
=References= | =References= | ||
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Revision as of 07:46, 17 March 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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IntroductionIntroduction
Orotidine monophosphate decarboxylase (ODCase), also known as orotidine 5’-monophosphate decarboxylase (OMP decarboxylase) or orotidine 5’-phosphate decarboxylase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the conversion of orotidine 5’-monophosphate (OMP) to uridine 5’-monophosphate (UMP). This reaction is the final step in de novo pyrimidine nucleotide synthesis and is an essential precursor for both DNA and RNA. The main structure of orotidine monophosphate decarboxylase is a TIM barrel, with one side acting as the binding site, while the other side is closed-off. This enzyme has been studied for it’s extreme catalytic proficiency[1].
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| 1dv7, resolution 1.80Å () | |||||||||
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| Activity: | Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 | ||||||||
| Related: | 1dvj | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Catalytic ReactionCatalytic Reaction
- first bullet
- sub-bullet
- second bullet[2]
- α
- category 1 [2]
- 2
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Protein StructureProtein Structure
TIM BarrelTIM Barrel
Active SiteActive Site
Rate of CatalysisRate of Catalysis
Substrate DestabilizationSubstrate Destabilization
ReferencesReferences
- ↑ Miller BG, Hassell AM, Wolfenden R, Milburn MV, Short SA. Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog. Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2011-6. PMID:10681417 doi:10.1073/pnas.030409797
- ↑ 2.0 2.1 Wu N, Mo Y, Gao J, Pai EF. Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase. Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2017-22. PMID:10681441 doi:10.1073/pnas.050417797
- ↑ Lee JK, Houk KN. A proficient enzyme revisited: the predicted mechanism for orotidine monophosphate decarboxylase. Science. 1997 May 9;276(5314):942-5. PMID:9139656