Alpha-ketoglutarate oxidoreductase, an essential salvage enzyme of energy metabolism, in coccoid form of Helicobacter pylori

Hitoshi Tsugawa, Hidekazu Suzuki, Izumi Nakagawa, Toshihiro Nishizawa, Yoshimasa Saito, Makoto Suematsu, Toshifumi Hibi

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

In the Krebs cycle of Helicobacter pylori, the absence of alpha-ketoglutarate dehydrogenase and succinyl CoA synthetase are shown. Instead, alpha-ketoglutarate is converted to succinyl CoA and succinate by alpha-ketoglutarate oxidoreductase (KOR) and CoA transferase (CoAT). In the present study, when H. pylori transformed to the coccoid form, a viable but non-culturable form of H. pylori with reduced metabolic activity, the KOR activity was enhanced while the CoAT activity was reduced. Direct inactivation of KOR could potently kill the bacteria without allowing conversion to the coccoid form, suggesting a novel treatment strategy for the eradication of H. pylori, especially in cases infected with multiple antibiotic-resistant strains.

Original languageEnglish
Pages (from-to)46-51
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume376
Issue number1
DOIs
Publication statusPublished - 2008 Nov 7

Fingerprint

2-oxoglutarate synthase
Coenzyme A-Transferases
Salvaging
Helicobacter pylori
Energy Metabolism
Oxidoreductases
Succinate-CoA Ligases
Ketoglutarate Dehydrogenase Complex
Succinic Acid
Enzymes
Bacteria
Anti-Bacterial Agents
Citric Acid Cycle

Keywords

  • Alpha-ketoglutarate oxidoreductase
  • CoA transferase
  • Coccoid form
  • Helicobacter pylori
  • Krebs cycle

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Alpha-ketoglutarate oxidoreductase, an essential salvage enzyme of energy metabolism, in coccoid form of Helicobacter pylori. / Tsugawa, Hitoshi; Suzuki, Hidekazu; Nakagawa, Izumi; Nishizawa, Toshihiro; Saito, Yoshimasa; Suematsu, Makoto; Hibi, Toshifumi.

In: Biochemical and Biophysical Research Communications, Vol. 376, No. 1, 07.11.2008, p. 46-51.

Research output: Contribution to journalArticle

Tsugawa, Hitoshi ; Suzuki, Hidekazu ; Nakagawa, Izumi ; Nishizawa, Toshihiro ; Saito, Yoshimasa ; Suematsu, Makoto ; Hibi, Toshifumi. / Alpha-ketoglutarate oxidoreductase, an essential salvage enzyme of energy metabolism, in coccoid form of Helicobacter pylori. In: Biochemical and Biophysical Research Communications. 2008 ; Vol. 376, No. 1. pp. 46-51.
@article{202b8bc210fe455888d8c9dd8d10e184,
title = "Alpha-ketoglutarate oxidoreductase, an essential salvage enzyme of energy metabolism, in coccoid form of Helicobacter pylori",
abstract = "In the Krebs cycle of Helicobacter pylori, the absence of alpha-ketoglutarate dehydrogenase and succinyl CoA synthetase are shown. Instead, alpha-ketoglutarate is converted to succinyl CoA and succinate by alpha-ketoglutarate oxidoreductase (KOR) and CoA transferase (CoAT). In the present study, when H. pylori transformed to the coccoid form, a viable but non-culturable form of H. pylori with reduced metabolic activity, the KOR activity was enhanced while the CoAT activity was reduced. Direct inactivation of KOR could potently kill the bacteria without allowing conversion to the coccoid form, suggesting a novel treatment strategy for the eradication of H. pylori, especially in cases infected with multiple antibiotic-resistant strains.",
keywords = "Alpha-ketoglutarate oxidoreductase, CoA transferase, Coccoid form, Helicobacter pylori, Krebs cycle",
author = "Hitoshi Tsugawa and Hidekazu Suzuki and Izumi Nakagawa and Toshihiro Nishizawa and Yoshimasa Saito and Makoto Suematsu and Toshifumi Hibi",
year = "2008",
month = "11",
day = "7",
doi = "10.1016/j.bbrc.2008.08.078",
language = "English",
volume = "376",
pages = "46--51",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Alpha-ketoglutarate oxidoreductase, an essential salvage enzyme of energy metabolism, in coccoid form of Helicobacter pylori

AU - Tsugawa, Hitoshi

AU - Suzuki, Hidekazu

AU - Nakagawa, Izumi

AU - Nishizawa, Toshihiro

AU - Saito, Yoshimasa

AU - Suematsu, Makoto

AU - Hibi, Toshifumi

PY - 2008/11/7

Y1 - 2008/11/7

N2 - In the Krebs cycle of Helicobacter pylori, the absence of alpha-ketoglutarate dehydrogenase and succinyl CoA synthetase are shown. Instead, alpha-ketoglutarate is converted to succinyl CoA and succinate by alpha-ketoglutarate oxidoreductase (KOR) and CoA transferase (CoAT). In the present study, when H. pylori transformed to the coccoid form, a viable but non-culturable form of H. pylori with reduced metabolic activity, the KOR activity was enhanced while the CoAT activity was reduced. Direct inactivation of KOR could potently kill the bacteria without allowing conversion to the coccoid form, suggesting a novel treatment strategy for the eradication of H. pylori, especially in cases infected with multiple antibiotic-resistant strains.

AB - In the Krebs cycle of Helicobacter pylori, the absence of alpha-ketoglutarate dehydrogenase and succinyl CoA synthetase are shown. Instead, alpha-ketoglutarate is converted to succinyl CoA and succinate by alpha-ketoglutarate oxidoreductase (KOR) and CoA transferase (CoAT). In the present study, when H. pylori transformed to the coccoid form, a viable but non-culturable form of H. pylori with reduced metabolic activity, the KOR activity was enhanced while the CoAT activity was reduced. Direct inactivation of KOR could potently kill the bacteria without allowing conversion to the coccoid form, suggesting a novel treatment strategy for the eradication of H. pylori, especially in cases infected with multiple antibiotic-resistant strains.

KW - Alpha-ketoglutarate oxidoreductase

KW - CoA transferase

KW - Coccoid form

KW - Helicobacter pylori

KW - Krebs cycle

UR - http://www.scopus.com/inward/record.url?scp=52049104187&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=52049104187&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2008.08.078

DO - 10.1016/j.bbrc.2008.08.078

M3 - Article

VL - 376

SP - 46

EP - 51

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -