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The burden borne by urease.

Brian P Callahan1, Yang Yuan, Richard Wolfenden

  • 1Department of Biochemistry & Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.

Journal of the American Chemical Society
|August 4, 2005
PubMed
Summary
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Urease is an exceptionally powerful enzyme catalyst. Experimental data reveals that the spontaneous hydrolysis of tetramethylurea is very slow, supporting urease

Area of Science:

  • Biochemistry
  • Enzymology
  • Physical Chemistry

Background:

  • Urea hydrolysis is crucial in biological systems, but its spontaneous rate is unknown due to ammonia elimination.
  • Quantum mechanical simulations suggest urea hydrolysis is extremely slow, implying urease is a highly potent enzyme catalyst.

Purpose of the Study:

  • To experimentally determine the spontaneous hydrolysis rate of urea and assess urease's catalytic power.
  • To investigate the hydrolysis of 1,1,3,3-tetramethylurea, a substrate resistant to ammonia elimination.

Main Methods:

  • Measured the uncatalyzed hydrolysis rate constant of 1,1,3,3-tetramethylurea in neutral solution at 25°C.
  • Compared the hydrolysis rates of tetramethylurea, acetamide, and N,N-dimethylacetamide.
  • Estimated the catalytic proficiency of urease using (kcat/Km)/knon.

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Main Results:

  • The rate constant for uncatalyzed tetramethylurea hydrolysis is 4.2 x 10^-12 s^-1.
  • This rate is comparable to other amides like acetamide and N,N-dimethylacetamide.
  • Urease exhibits a catalytic proficiency of 8 x 10^17 M^-1, exceeding other metalloenzymes.

Conclusions:

  • Spontaneous urea hydrolysis is significantly slower than previously assumed.
  • Urease demonstrates remarkable catalytic efficiency, surpassing other known enzymes in accelerating urea hydrolysis.
  • The findings validate the exceptional catalytic power attributed to urease.