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J Med Microbiol 46 (1997), 793-800; DOI: 10.1099/00222615-46-9-793
© 1997 Society for General Microbiology
ISSN 0022-2615
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Amino acid utilisation and deamination of glutamine and asparagine by Helicobacter pylori

R. M. STARK, M.-S. SULEIMAN*, I. J. HASSAN{dagger}, J. GREENMAN and M. R. MILLAR{dagger}

Faculty of Science, Department of Biological Sciences, University of the West of England, Coldharbour Lane, Frenchay, Bristol BS16 1QY

*Department of Cardiac Surgery, University of Bristol, Bristol Royal Infirmary, Marlborough Street, Bristol BS2 8HW

{dagger}Department of Pathology and Microbiology, University of Bristol, Bristol Royal Infirmary, Marlborough Street, Bristol BS2 8HW

Corresponding author: Dr M. R. Millar.

Received November 1, 1996 Revision received February 17, 1997.
Accepted February 17, 1997

Helicobacter pylori can utilise amino acids as the sole carbon energy source. The present study demonstrated that H. pylori grown in continuous culture in a defined medium containing glucose and amino acids utilised alanine, arginine, asparagine, aspartate, glutamine, glutamate, proline and serine. Specific asparaginase and glutaminase enzymes deaminated asparagine and glutamine respectively to aspartate and glutamate, with the production of ammonia. The glutaminase activity was inhibited by 6-diazo-5-oxo-L-norleucine. All the 13 strains of H. pylori tested produced both glutaminase and asparaginase activities. Glutamine is important in the health of the gastric and intestinal mucosa and is a primary energy source for lymphocytes. Depletion of glutamine at the site of H. pylori infection may be of significance in the pathogenesis of H. pylori-associated diseases such as peptic ulcer and gastric cancer.




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