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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 1 Introduction 2 Structure 2.1 TIM Barrel 2.2 Active Site 3 Function 3.1 UMP Synthase 4 Rate of Catalysis 4.1 Substrate Destabilization 5 References

spinqualitylabelsall models PDB ID 1dv7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1dv7, resolution 1.80Å ()
Activity:	Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23
Related:	1dvj
Structural annotation: Resources: CATH : 1Dv7A00 InterPro : Ipr011060, Ipr014732, Ipr001754, Ipr013785 Pfam : PF00215 SCOP : d1dv7a_ UniProt : O26232
Functional annotation: Biological process: pyrimidine nucleotide biosynthetic process 'de novo' pyrimidine base biosynthetic process metabolic process Molecular function: carboxy-lyase activity orotidine-5'-phosphate decarboxylase activity catalytic activity lyase activity
Evolutionary conservation: Toggle Conservation Colors: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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