author_facet Nagata, Kumiko
Nagata, Yoko
Sato, Tadashi
Fujino, Masayuki A.
Nakajima, Kazuhiko
Tamura, Toshihide
Nagata, Kumiko
Nagata, Yoko
Sato, Tadashi
Fujino, Masayuki A.
Nakajima, Kazuhiko
Tamura, Toshihide
author Nagata, Kumiko
Nagata, Yoko
Sato, Tadashi
Fujino, Masayuki A.
Nakajima, Kazuhiko
Tamura, Toshihide
spellingShingle Nagata, Kumiko
Nagata, Yoko
Sato, Tadashi
Fujino, Masayuki A.
Nakajima, Kazuhiko
Tamura, Toshihide
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
Microbiology
author_sort nagata, kumiko
spelling Nagata, Kumiko Nagata, Yoko Sato, Tadashi Fujino, Masayuki A. Nakajima, Kazuhiko Tamura, Toshihide 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.26203-0 <jats:p><jats:italic>Helicobacter pylori</jats:italic>whole cells showed high rates of oxygen uptake with<jats:sc>l</jats:sc>-serine and<jats:sc>l</jats:sc>-proline as respiratory substrates, and somewhat lower rates with<jats:sc>d</jats:sc>-alanine and<jats:sc>d</jats:sc>-proline. These respiratory activities were inhibited by rotenone and antimycin A at low concentrations. Since pyruvate was produced from<jats:sc>l</jats:sc>-serine and<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-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<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline and<jats:sc>d</jats:sc>-alanine as substrates, suggesting that hydrogen removed from these amino acids also participated in oxygen uptake by the whole cells. High amounts of<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-alanine, and<jats:sc>l</jats:sc>-serine were present in<jats:italic>H. pylori</jats:italic>cells, and these amino acids also predominated in samples of human gastric juice.<jats:italic>H. pylori</jats:italic>seems to utilize<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>-alanine and<jats:sc>l</jats:sc>-serine as important energy sources in its habitat of the mucous layer of the stomach.</jats:p> l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels Microbiology
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title l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_unstemmed l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_full l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_fullStr l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_full_unstemmed l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_short l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_sort l-serine, d- and l-proline and alanine as respiratory substrates of helicobacter pylori: correlation between in vitro and in vivo amino acid levels
topic Microbiology
url http://dx.doi.org/10.1099/mic.0.26203-0
publishDate 2003
physical 2023-2030
description <jats:p><jats:italic>Helicobacter pylori</jats:italic>whole cells showed high rates of oxygen uptake with<jats:sc>l</jats:sc>-serine and<jats:sc>l</jats:sc>-proline as respiratory substrates, and somewhat lower rates with<jats:sc>d</jats:sc>-alanine and<jats:sc>d</jats:sc>-proline. These respiratory activities were inhibited by rotenone and antimycin A at low concentrations. Since pyruvate was produced from<jats:sc>l</jats:sc>-serine and<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-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<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline and<jats:sc>d</jats:sc>-alanine as substrates, suggesting that hydrogen removed from these amino acids also participated in oxygen uptake by the whole cells. High amounts of<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-alanine, and<jats:sc>l</jats:sc>-serine were present in<jats:italic>H. pylori</jats:italic>cells, and these amino acids also predominated in samples of human gastric juice.<jats:italic>H. pylori</jats:italic>seems to utilize<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>-alanine and<jats:sc>l</jats:sc>-serine as important energy sources in its habitat of the mucous layer of the stomach.</jats:p>
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author Nagata, Kumiko, Nagata, Yoko, Sato, Tadashi, Fujino, Masayuki A., Nakajima, Kazuhiko, Tamura, Toshihide
author_facet Nagata, Kumiko, Nagata, Yoko, Sato, Tadashi, Fujino, Masayuki A., Nakajima, Kazuhiko, Tamura, Toshihide, Nagata, Kumiko, Nagata, Yoko, Sato, Tadashi, Fujino, Masayuki A., Nakajima, Kazuhiko, Tamura, Toshihide
author_sort nagata, kumiko
container_issue 8
container_start_page 2023
container_title Microbiology
container_volume 149
description <jats:p><jats:italic>Helicobacter pylori</jats:italic>whole cells showed high rates of oxygen uptake with<jats:sc>l</jats:sc>-serine and<jats:sc>l</jats:sc>-proline as respiratory substrates, and somewhat lower rates with<jats:sc>d</jats:sc>-alanine and<jats:sc>d</jats:sc>-proline. These respiratory activities were inhibited by rotenone and antimycin A at low concentrations. Since pyruvate was produced from<jats:sc>l</jats:sc>-serine and<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-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<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline and<jats:sc>d</jats:sc>-alanine as substrates, suggesting that hydrogen removed from these amino acids also participated in oxygen uptake by the whole cells. High amounts of<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-alanine, and<jats:sc>l</jats:sc>-serine were present in<jats:italic>H. pylori</jats:italic>cells, and these amino acids also predominated in samples of human gastric juice.<jats:italic>H. pylori</jats:italic>seems to utilize<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>-alanine and<jats:sc>l</jats:sc>-serine as important energy sources in its habitat of the mucous layer of the stomach.</jats:p>
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spelling Nagata, Kumiko Nagata, Yoko Sato, Tadashi Fujino, Masayuki A. Nakajima, Kazuhiko Tamura, Toshihide 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.26203-0 <jats:p><jats:italic>Helicobacter pylori</jats:italic>whole cells showed high rates of oxygen uptake with<jats:sc>l</jats:sc>-serine and<jats:sc>l</jats:sc>-proline as respiratory substrates, and somewhat lower rates with<jats:sc>d</jats:sc>-alanine and<jats:sc>d</jats:sc>-proline. These respiratory activities were inhibited by rotenone and antimycin A at low concentrations. Since pyruvate was produced from<jats:sc>l</jats:sc>-serine and<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-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<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline and<jats:sc>d</jats:sc>-alanine as substrates, suggesting that hydrogen removed from these amino acids also participated in oxygen uptake by the whole cells. High amounts of<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-alanine, and<jats:sc>l</jats:sc>-serine were present in<jats:italic>H. pylori</jats:italic>cells, and these amino acids also predominated in samples of human gastric juice.<jats:italic>H. pylori</jats:italic>seems to utilize<jats:sc>d</jats:sc>- and<jats:sc>l</jats:sc>-proline,<jats:sc>d</jats:sc>-alanine and<jats:sc>l</jats:sc>-serine as important energy sources in its habitat of the mucous layer of the stomach.</jats:p> l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels Microbiology
spellingShingle Nagata, Kumiko, Nagata, Yoko, Sato, Tadashi, Fujino, Masayuki A., Nakajima, Kazuhiko, Tamura, Toshihide, 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, Microbiology
title l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_full l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_fullStr l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_full_unstemmed l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_short l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_sort l-serine, d- and l-proline and alanine as respiratory substrates of helicobacter pylori: correlation between in vitro and in vivo amino acid levels
title_unstemmed l-Serine, d- and l-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
topic Microbiology
url http://dx.doi.org/10.1099/mic.0.26203-0