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The appearance of enzyme activity for D-amino acid in highly concentrated ammonium phosphate solution

Research Project

Project/Area Number 06680551
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Bioorganic chemistry
Research InstitutionUniversity of Tsukuba

Principal Investigator

SHIMADA Akihiko  Univeristy of Tsukuba, Institution of Applied Biochemistry, assistant Professor, 応用生物化学系, 講師 (90235614)

Project Period (FY) 1994 – 1996
Project Status Completed (Fiscal Year 1996)
Budget Amount *help
¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1996: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1995: ¥600,000 (Direct Cost: ¥600,000)
Keywordsorigin of optical activity / selection mechanism for optical isomers on enzyme / D-tryptophan / tryptophanase / diammoniumhydrogen phosphate / 光学活性の起源 / リン酸水素2アンモニウム / 生命の起原 / アミノ酸光学異性体の選択
Research Abstract

We had elucidated the reaction pathway of tryptophanase-catalysed degradation of D-tryptophan in the presence of diammoniumhydrogen phosphate and had studied selection mechanism of D-amino acids on enzyme for the term of this project. Information newly obtained from this research is described below.
1.Diammoniumhydrogen phosphate ((NH_4) _2HPO_4) acted on tryptophanase as an activator below 50% saturation, but as a noncompetitive inhibitor above 50% saturation.
2.Reaction pathway was satisfactorily clarified on the basis of kinetic analysis. Tryptophanase bound at random with D-tryptophan and (NH_4) _2HPO_4 in rapid equilibrium. D-tryptophan was degraded through tryptophnase・D-tryptophan・ (NH_4) _2HPO_4 complex.
3.D-tryptophan bound with tryptophanase in the absence of (NH_4) _2HPO_4. Increasing concentration of (NH_4) _2HPO_4 changed inhibition type from competitive type through mixed type to uncompetitive type.
4.The above result indicated that binding site and catalytic site within active site of tryptophanase was independent. In addition, it was suggested that the binding site of D-tryptophan independently behaved for that of L-tryptophan.
5.Results so far obtained have been reported in papers.

Report

(4 results)
  • 1996 Annual Research Report   Final Research Report Summary
  • 1995 Annual Research Report
  • 1994 Annual Research Report
  • Research Products

    (16 results)

All Other

All Publications (16 results)

  • [Publications] 島田秋彦: "トリプトファナーゼのD-トリプトファンに対する反応機構の動力学的解析" Viva Origino. 23. 169-178 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] 島田秋彦: "Reaction mechanism to D-tryptophan in tryptopanase" Amino Acids. 9. 24-24 (1995)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] 島田秋彦: "Tryptophanase-catalysed degradation of d-tryptophan in highly concentrated diammonium hydrogen phosphate solution" Amino Acids. 11. 83-89 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] 島田秋彦: "トリプトファナーゼにおけるD-トリプトファンの活性部位の反応速度論による検討" Viva Origino. (印刷中). (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] 島田秋彦: "Reaction pathway of tryptophanase degrading D-tryptophan" Amino Acids. (印刷中). (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Shimad A.: "Kinetic analysis of mechanism in reaction of tryptophanase with D-tryptophan" Viva Origino. 23. 169-178 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Shimada A.: "Reaction mechanism to D-tryptophan in tryptophanase" Amino Acids. 9. 24 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Shimada A.: "Tryptophanase-catalysed degradation of D-tryptophan in highly concentrated diammonium hydrogen phosphate solution" Amino Acids. 11. 83-89 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Shimada A.: "Kinetic investigation of active site for D-tryptophan on tryptophanase" Viva Origino. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Shimada A.: "Reaction pathway of tryptophanase degrading D-tryptophan" Amino Acids. (in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] 島田 秋彦: "Tryptophanase-catalysed degradation of D-tryptophan in highly concentrated diammonium hydrogen phosphate solution" Amino Acids. 11. 83-89 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] 島田 秋彦: "トリプトファナーゼにおけるD-トリプトファンの活性部位の反応速度論による検討" Viva Origino. (印刷中). (1997)

    • Related Report
      1996 Annual Research Report
  • [Publications] 島田 秋彦: "Reaction Pathway of tryptophanase degrading D-tryptophan" Amino Acids. (印刷中). (1997)

    • Related Report
      1996 Annual Research Report
  • [Publications] 島田秋彦: "トリプトファナーゼのD-トリプトファンに対する反応機構の動力学的解析" Viva Orgino. 23. 169-178 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] 島田秋彦: "Reaction mechanism to D-tryptophan in tryptophanase" Amino Acids. 9. 24-24 (1995)

    • Related Report
      1995 Annual Research Report
  • [Publications] 島田秋彦: "リン酸アンモニウム存在下でのトリプトファナーゼによる光学異性体選択の変化" Viva Origino. 22. 26-27 (1994)

    • Related Report
      1994 Annual Research Report

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Published: 1995-04-01   Modified: 2016-04-21  

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