Sandbox Reserved 315

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<scene name='Sandbox_Reserved_315/Practice_representation/1'>Representation</scene>
<scene name='Sandbox_Reserved_315/Practice_representation/1'>Representation</scene>
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=Catalytic Reaction=
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=Structure=
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==TIM Barrel==
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==Active Site==
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[http://www.wikipedia.org Wikipedia]
[http://www.wikipedia.org Wikipedia]
<Structure load=1dv7 size='200' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_315/Practice_representation/1'/>
<Structure load=1dv7 size='200' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_315/Practice_representation/1'/>
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=Protein Structure=
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=Function=
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==TIM Barrel==
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==UMP Synthase==
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==Active Site==
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=Rate of Catalysis=
=Rate of Catalysis=
==Substrate Destabilization==
==Substrate Destabilization==

Revision as of 05:38, 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.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

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[1].

Contents


PDB ID 1dv7

Drag the structure with the mouse to rotate
1dv7, resolution 1.80Å ()
Activity: Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23
Related: 1dvj
Resources: FirstGlance, OCA, RCSB, PDBsum, TOPSAN
Coordinates: save as pdb, mmCIF, xml


Structure

TIM Barrel

Active Site

  • first bullet
    • sub-bullet
  • second bullet[2]
    • α
  1. category 1 [2]
    1. 2

Wikipedia

Insert caption here

Drag the structure with the mouse to rotate

Function

UMP Synthase

Rate of Catalysis

Substrate Destabilization

[3]

References

  1. ↑ 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. ↑ 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
  3. ↑ 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
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