Sandbox Reserved 315: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 22: Line 22:
#category 1 <Ref name = "Wu">PMID:10681441</ref>
#category 1 <Ref name = "Wu">PMID:10681441</ref>
##2
##2
[http://www.wikipedia.org Wikipedia]
 


=Function=
=Function=
<Structure load=1dv7 size='200' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_315/Odcase_dimer/1'/>
<Structure load=1dv7 size='200' frame='true' align='left' caption='Insert caption here' scene='Sandbox_Reserved_315/Odcase_dimer/1'/>
==UMP Synthase==
==UMP Synthase==
In multicellular eukaryotes, orotidine monophosphate decarboxylase associates with orotate phosphoribosyltransferase to form a bifunctional protein, [[UMP synthase]]<Ref name = "Lee"/><Ref name = "Yablonski"/>. UMP synthase carries out the last two steps in pyrimidine biosynthesis, converting orotate to uridine 5'-monophosphate<Ref name = "Yablonski">PMID:8631878</ref>. This reaction involves first adding ribose-P to orotate to form orotidine 5'-monophosphate, followed by a decarboxylation reaction to form uridine 5'-monophosphate<Ref name = "Yablonski"/>. In microorganisms these two enzymes are separate and coded by distinct genes. However research has shown that all multicellular eukaryotes so far code the genes for these two enzymes together and as a result they are covalently bonded as a bifunctional protein with two distinct catalytic domains<Ref name = "Yablonski"/>.  
In multicellular eukaryotes, orotidine monophosphate decarboxylase associates with orotate phosphoribosyltransferase to form a bifunctional protein, uridine monophosphate synthase ([http://en.wikipedia.org/wiki/Uridine_monophosphate_synthetase UMP Synthase])<Ref name = "Lee"/><Ref name = "Yablonski"/>. UMP synthase carries out the last two steps in pyrimidine biosynthesis, converting orotate to uridine 5'-monophosphate<Ref name = "Yablonski">PMID:8631878</ref>. This reaction involves first adding ribose-P to orotate to form orotidine 5'-monophosphate, followed by a decarboxylation reaction to form uridine 5'-monophosphate<Ref name = "Yablonski"/>. In microorganisms these two enzymes are separate and coded by distinct genes. However research has shown that all multicellular eukaryotes so far code the genes for these two enzymes together and as a result they are covalently bonded as a bifunctional protein with two distinct catalytic domains<Ref name = "Yablonski"/>.  
=Rate of Catalysis=
=Rate of Catalysis=
==Substrate Destabilization==
==Substrate Destabilization==

Revision as of 09:33, 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

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].


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


StructureStructure

TIM BarrelTIM Barrel

Active SiteActive Site

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


FunctionFunction

Insert caption here

Drag the structure with the mouse to rotate

UMP SynthaseUMP Synthase

In multicellular eukaryotes, orotidine monophosphate decarboxylase associates with orotate phosphoribosyltransferase to form a bifunctional protein, uridine monophosphate synthase (UMP Synthase)[3][4]. UMP synthase carries out the last two steps in pyrimidine biosynthesis, converting orotate to uridine 5'-monophosphate[4]. This reaction involves first adding ribose-P to orotate to form orotidine 5'-monophosphate, followed by a decarboxylation reaction to form uridine 5'-monophosphate[4]. In microorganisms these two enzymes are separate and coded by distinct genes. However research has shown that all multicellular eukaryotes so far code the genes for these two enzymes together and as a result they are covalently bonded as a bifunctional protein with two distinct catalytic domains[4].

Rate of CatalysisRate of Catalysis

Substrate DestabilizationSubstrate Destabilization

[3]

ReferencesReferences

  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. ↑ 3.0 3.1 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
  4. ↑ 4.0 4.1 4.2 4.3 Yablonski MJ, Pasek DA, Han BD, Jones ME, Traut TW. Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase. J Biol Chem. 1996 May 3;271(18):10704-8. PMID:8631878

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Sarah Geisheimer
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=Sandbox_Reserved_315&oldid=1216196"