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Analysis of an enzymatic domain that is involved in specificity of phosphoryl donors, polyphosphate and ATP

Research Project

Project/Area Number 15560676
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Biofunction/Bioprocess
Research InstitutionHIROSHIMA UNIVERSITY

Principal Investigator

KURODA Akio  Hiroshima University, Graduate school of advanced sciences of matter, Associate professor, 大学院・先端物質科学研究科, 助教授 (50205241)

Project Period (FY) 2003 – 2004
Project Status Completed (Fiscal Year 2004)
Budget Amount *help
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2004: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2003: ¥2,600,000 (Direct Cost: ¥2,600,000)
Keywordspolyphospahte / glucokinase / ATP / evolution / life energy / structure analysis / 結晶 / リン酸化 / 基質特異性 / タンパク質工学
Research Abstract

Inorganic polyphosphate (polyP) is a linear polymer of phosphate linked by high energy phosphoanhydride bonds. PolyP is found in abundance in volcanic condensates. Therefore, some investigators consider that polyP may be energy currency for prebiotic life. We found that a strictly polyP-dependent glucokinase in Microlunatus phosphovorus. ATP is used to phosphorylate glucose in many organisms, while polyP is used in this microorganism. We determined a primary structure of this polyP-glucokinase, and found that the active site residues are conserved in both of ATP- and polyP-glucokinase. However, a domain IIB is only observed in ATP-glucokinase. We considered that ATP-glucokinase is evolved from polyP-glucokinase. In this study, we wanted to reveal structural changes in glucokinase when it acquire the domain IIB and changes its phosphoryl donor. First we purified polyP-glucokinase from E.coli recombinant. The purified enzyme is further concentrated and used in order to find crystalization condition. Finally we succeeded in crystalization of polyP-glucokinase and obtaining X-ray diffraction pattern with two-angstrom resolution. We have not yet solved, but succeeded in predicting its three-dimensional structure. We predicted that polyP-glucokinase acquired adenosine recognizing domain and evolved to ATP-glucokinase.

Report

(3 results)
  • 2004 Annual Research Report   Final Research Report Summary
  • 2003 Annual Research Report
  • Research Products

    (4 results)

All 2004 Other

All Journal Article (2 results) Publications (2 results)

  • [Journal Article] 微生物のポリリン酸研究の新展開2004

    • Author(s)
      黒田章夫
    • Journal Title

      日本農芸化学会誌 78

      Pages: 738-743

    • NAID

      10013521360

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Annual Research Report 2004 Final Research Report Summary
  • [Journal Article] New Aspects of Polyphosphate Functions and Applications in Microorganisms2004

    • Author(s)
      Akio Kuroda
    • Journal Title

      Nougei-Kagaku Kaishi 78

      Pages: 738-743

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Publications] Tanaka S. et al.: "Strictly polyphosphate-dependent glucokinase in a polyphosphate-accumulating bacterium Microlunatus phosphovorus"Journal of Bacteriology. 185. 5654-5656 (2003)

    • Related Report
      2003 Annual Research Report
  • [Publications] 黒田章夫: "微生物におけるポリリン酸代謝制御機構の解明と利用"生物工学会誌. 81. 104-111 (2003)

    • Related Report
      2003 Annual Research Report

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Published: 2003-04-01   Modified: 2016-04-21  

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