A proficient enzyme.

@article{Radzicka1995APE,
  title={A proficient enzyme.},
  author={Anna Radzicka and Richard Wolfenden},
  journal={Science},
  year={1995},
  volume={267 5194},
  pages={
          90-3
        }
}
Orotic acid is decarboxylated with a half-time (t1/2) of 78 million years in neutral aqueous solution at room temperature, as indicated by reactions in quartz tubes at elevated temperatures. Spontaneous hydrolysis of phosphodiester bonds, such as those present in the backbone of DNA, proceeds even more slowly at high temperatures, but the heat of activation is less positive, so that dimethyl phosphate is hydrolyzed with a t1/2 of 130,000 years in neutral solution at room temperature. These… 
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648 Citations
Highly Influential Citations
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Background Citations
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Methods Citations
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648 Citations

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Current proposals for the mechanism of enzymatic decarboxylation are discussed in light of recent computational, structural, and mutagenesis studies.
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Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog.
TLDR
Interactions between the enzyme and the phosphoribosyl group anchor the pyrimidine within the active site, helping to explain the phosphorus group's remarkably large contribution to catalysis despite its distance from the site of decarboxylation.
The Depth of Chemical Time and the Power of Enzymes as
TLDR
Thermodynamic comparisons between spontaneous and enzyme-catalyzed reactions, coupled with structural information, suggest that in addition to electrostatic and H-bonding interactions, the liberation of water molecules from an enzyme’s active site into bulk solvent sometimes plays a prominent role in determining the relative binding affinities of the altered substrate in the ground state and transition state.
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CaaD achieves an approximately 10(12)-fold rate enhancement, matching or surpassing the rate enhancements produced by many enzymes that act on more conventional biological substrates, including 4-oxalocrotonate tautomerase, with which CaaD seems to share a common evolutionary origin.
Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.
TLDR
The enzyme OMPDC has posed a challenge to the enzymologist attempting to explain a 1017-fold rate acceleration in the absence of cofactors or even metal ions, so a comparison of the available evidence on the three types of decarboxylases underlines some common features and more differences.
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TLDR
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TLDR
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