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Related Experiment Videos

Rat liver imidase

Y S Yang1, S Ramaswamy, W B Jakoby

  • 1Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.

The Journal of Biological Chemistry
|May 25, 1993
PubMed
Summary
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Rat liver imidase, also known as dihydropyrimidinase, purifies to homogeneity. This enzyme broadens its role beyond pyrimidine metabolism to xenobiotic detoxification, catalyzing hydrolytic cleavage of various imides.

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Imidase, identified as dihydropyrimidinase (EC 3.5.2.2), hydantoinase, dihydropyrimidine hydrase, and dihydropyrimidine amidohydrolase, is crucial in pyrimidine metabolism.
  • Its role extends to the detoxification of xenobiotics, highlighting its broader physiological significance.

Purpose of the Study:

  • To purify imidase from rat liver to electrophoretic homogeneity.
  • To characterize the enzyme's substrate specificity and catalytic properties.
  • To propose a mechanism for the enzyme-catalyzed reaction.

Main Methods:

  • Purification of imidase from rat liver to electrophoretic homogeneity.
  • Enzyme kinetics studies to determine substrate range and pH dependence.
  • Investigation of stereoselectivity and stereospecificity.

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Main Results:

  • Imidase was successfully purified to electrophoretic homogeneity from rat liver.
  • The enzyme catalyzes the hydrolytic cleavage of a diverse range of imides, including hydantoins, dihydropyrimidines, and phthalimide.
  • Enzyme activity is pH-dependent, correlating with substrate pKa values, and exhibits stereoselectivity and stereospecificity.

Conclusions:

  • Purified rat liver imidase functions in both pyrimidine catabolism and xenobiotic detoxification.
  • The enzyme's broad substrate range and stereospecificity suggest significant physiological and toxicological roles.
  • A proposed mechanism provides insight into the imidase-catalyzed reaction pathway.