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Oxygen sensitive pyruvate formate-lyase and its activating enzyme in oral microorganisms.

Research Project

Project/Area Number 04671120
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field Functional basic dentistry
Research InstitutionTOHOKU UNIVERSITY

Principal Investigator

ABE Kazuhiko  Tohoku Univ, School of Dentistry, Associate Professor., 歯学部, 助教授 (40151089)

Project Period (FY) 1992 – 1994
Project Status Completed (Fiscal Year 1994)
Budget Amount *help
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1993: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1992: ¥1,200,000 (Direct Cost: ¥1,200,000)
KeywordsPyruvate formate-lyase / Streptococcus mutans / Streptococcus sanguis / Acid production / Sorbitol / PFL activating enzyme / Selenium / PFL inactivating enzyme / ピルビン酸ギ酸リアーゼ / Streptococcus mutanら / 糖代謝 / スクロース / NADH / 歯垢 / ピルビン酸ギ酸リアーゼ活性化酵素 / ピルビン酸ギ酸リアーゼ不活性化酵素 / 嫌気糖代謝 / 酸素感受性酵素 / NADPH / 口腔レンサ球菌 / 高度嫌気条件
Research Abstract

Pyruvate formate-lyase (PFL) is a key enzyme of production of formic and acetic acid and ethanol by streptococci under anaerobic conditions. PFL was converted between oxygen-sensitive, active and oxygen tolerant, inactive forms in the cells of Streptococcus sanguis but not in the cells of Streptococcus mutans. All PFL was kept active in S.mutans cells. The biochmical mechanism of this difference in the interconversion was investigated. NADPH was the most efficient reducing agent for the activation of the inactive PFL of S.mutans. On the contrary, NADPH was not so efficient in S.sanguis. Fe^<2+> and selenium were required for PFL activating enzyme, and protein radial was involved in the active center of PFL.PFL inactivating enzyme, which converted active form to oxygen-tolerant inactive form, was found in streptococci. S.sanguis had higher activity of PFL inactivating enzyme than S.mutans.
Intracellular conversion of PFL could be explained by these findings. Minute levels of pyruvate and inorganic phosphate inhibited the activity of PFL inactivating enzyme and kept active form of PFL.However, CoA enhanced PFL inactivation. These regulatory mechanism could be important teleologically. Glucose or sucrose metabolism was inhibited by sorbitol in S.mutans under certain conditions. The incorporation of sorbitol resulted in high NADH/NAD ratio and inhibited streptococcal sugar metabolism, since PFL activity was not enough to keep the oxidation/reduction balance. Sorbitol also inhibited sugar metabolism of microorganisms in dental plaque in situ.

Report

(4 results)
  • 1994 Annual Research Report   Final Research Report Summary
  • 1993 Annual Research Report
  • 1992 Annual Research Report
  • Research Products

    (16 results)

All Other

All Publications (16 results)

  • [Publications] K.Abbe: "Activation and inactivation of pyruvate formate-lyase in oral streptococci." J.Dent.Res.71(S). 695- (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Y.Iwami: "Acid production by streptococci growing at low pH in a chemostat under anaerobic conditions." Oral Microbiol.Immunol.7. 304-308 (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] 阿部,一彦: "Streptococcus mutansのピルビン酸ギ酸リアーゼの活性化酵素の性質" 歯科基礎誌. 34(補). 73- (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] 阿部,一彦: "連鎖球菌ピルビン酸ギ酸リアーゼの酸素耐性な可逆的不活性型への変換酵素(PFL不活性化酵素)" 歯科基礎誌. 35(補). 195- (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] 阿部,一彦: "歯科細菌のスクロースまたはグルコース代謝に対するソルビトールの抑制効果に関する研究" 歯科基礎誌. 36(補). 90- (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] K.Abe: "Activation and inactivation of pyruvate formate-lyase in oral streptococci." J.Dent.Res.71 (S). 695- (1992)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Y.Iwami: "Acid production by streptococci growing low pH in a chemostat under anaerobic conditions." Oral Microbiol. Immunol.7. 304-308 (1992)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] P.Zhang: "Acidogenicity of oral throat lozenges available in Japan." J.Dent.Res.(printing).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] K.Abe: "Sorbitol inhibition on sugar metabolism of plaque microorganisms." J.Dent.Res.(printing).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] 阿部,一彦: "歯垢細菌のスクロースまたはグルコース代謝に対するソルビトールの抑制効果に関する研究" 歯科基礎誌. 36(補). 90- (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] P.Zhang: "Acidogenicity of oral throat lozenges arailable in Japan." J.Dent.Res.(印刷中).

    • Related Report
      1994 Annual Research Report
  • [Publications] K.Abbe: "Sorbitol inhibition on sagar metabolism of plague microorganisms" J.Dent Res.(印刷中).

    • Related Report
      1994 Annual Research Report
  • [Publications] 阿部一彦: "連鎖球菌ピルビン酸ギ酸リアーゼの酸素耐性な可逆的不活性型への変換酵素(PFL不活性化酵素)" 歯科基礎医学会雑誌. 35S. 195 (1993)

    • Related Report
      1993 Annual Research Report
  • [Publications] Y.Iwami: "Acid production by streptococci growing at low pH in a chemostat under anaerobic conditions." Oral Microbiol.Immunol.7. 304-308 (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] K.Abbe: "Activation and inactivation of pyruvate formate-lyase in oral streptococci." J.Dent.Res.71. 695- (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] 阿部 一彦: "Streptococcus mutansのピルビン酸ギ酸リアーゼの活性化酵素の性質" 歯基礎誌. 34. 73- (1992)

    • Related Report
      1992 Annual Research Report

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Published: 1992-04-01   Modified: 2016-04-21  

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