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Avian mitochondrial glutamine metabolism.
The Journal of Biological Chemistry
|February 10, 1976
Summary
Avian liver mitochondria synthesize glutamine from glutamate without external ATP. This mitochondrial glutamine synthetase converts intramitochondrial ammonia into glutamine for uric acid biosynthesis.
Area of Science:
- Biochemistry
- Cell Biology
- Animal Physiology
Background:
- Avian liver mitochondria possess glutamine synthetase.
- Ammonia detoxification is crucial for purine biosynthesis.
Purpose of the Study:
- To investigate glutamine synthesis from glutamate in avian liver mitochondria.
- To determine the role of mitochondrial glutamine synthetase in ammonia detoxification.
Main Methods:
- Using L-[U-14C]glutamate and L-[15N]glutamate as substrates.
- Measuring 14CO2 release for glutamate deamination.
- Employing mass spectrometry to analyze glutamine.
- Studying L-glutamine permeability using rapid centrifugation.
Main Results:
- Mitochondria synthesized glutamine from glutamate without exogenous ATP or ammonia.
- A 1:1 stoichiometry was observed between glutamate deamination and amidation.
- 15N was incorporated into both alpha-amino and amide groups of glutamine.
- L-glutamine transport across the mitochondrial membrane is rapid and passive.
- Mitochondrial glutamine synthetase converts intramitochondrial ammonia to glutamine.
Conclusions:
- Mitochondrial glutamine synthetase is the primary site of ammonia detoxification in avian liver.
- Synthesized glutamine is effluxed to the cytosol for purine (uric acid) biosynthesis.