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Microbiology 149 (2003), 2023-2030; DOI  10.1099/mic.0.26203-0
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Microbiology 149 (2003), 2023-2030; DOI  10.1099/mic.0.26203-0
© 2003 Society for General Microbiology

L-Serine, D- and L-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels

Kumiko Nagata1, Yoko Nagata2, Tadashi Sato3, Masayuki A. Fujino3, Kazuhiko Nakajima1 and Toshihide Tamura1

1 Department of Bacteriology, Hyogo College of Medicine, 1-1 Mukogawa, Nishinomiya, Hyogo 663-8501, Japan
2 Department of Materials and Applied Chemistry, College of Science and Technology, Nihon University, 1-8-14 Kanda, Surugadai, Chiyoda-ku, Tokyo 101-8308, Japan
3 First Department of Medicine, Yamanashi Medical University, Kofu, Yamanashi, 409-3898, Japan

Correspondence
Kumiko Nagata
kunagata{at}hyo-med.ac.jp

Helicobacter pylori whole cells showed high rates of oxygen uptake with L-serine and L-proline as respiratory substrates, and somewhat lower rates with D-alanine and D-proline. These respiratory activities were inhibited by rotenone and antimycin A at low concentrations. Since pyruvate was produced from L-serine and D- and L-alanine in whole cells, the respiratory activities with these amino acids as substrates occurred via pyruvate. Whole cells showed 2,6-dichlorophenolindophenol (DCIP)-reducing activities with D- and L-proline and D-alanine as substrates, suggesting that hydrogen removed from these amino acids also participated in oxygen uptake by the whole cells. High amounts of L-proline, D- and L-alanine, and L-serine were present in H. pylori cells, and these amino acids also predominated in samples of human gastric juice. H. pylori seems to utilize D- and L-proline, D-alanine and L-serine as important energy sources in its habitat of the mucous layer of the stomach.


Abbreviations: DCPIP, 2,6-dichlorophenolindophenol




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