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Nutrition. 2002 Jun;18(6):455-7.

Hepatic glutaminase--a special role in urea synthesis?

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Department of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland A1B 3X9, Canada.



To investigate the relationship between hepatic glutaminase and the urea cycle with particular reference to the possibility of the existence of a metabolic channel between glutaminase and carbamylphosphate synthetase I (CPS-I).


Rat livers were perfused in the non-recirculating mode with 15-N labeled ammonia and glutamine. The incorporation of 15-N into nitrogenous products was determined by gas chromatography-mass spectrometry.


We devised and validated a theoretical framework that described the incorporation of the 15-N into the various urea mass isotopomers as a function of the isotopic abundance of 15-N in the two precursor molecules, aspartate and citrulline. We then compared the incorporation of 15-N from amino-labeled and amide-labeled glutamine. Glucagon activated incorporation of these labels into products, consistent with an activation of glutaminase. However, the results indicated no metabolic channel between glutaminase and CPS-I.


We suggest that glutaminase may play a role in promoting urea production by virtue of N-acetylglutamate synthesis rather than by a channeling mechanism. Glutaminase may provide glutamate, a substrate for the synthesis of N-acetylglutamate which is an obligatory activator of CPS-1.

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