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Characterization of Highly Functional Phospholipase D Produced by Streptoverticillium cinnamoneum

Research Project

Project/Area Number 10650786
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 生物・生体工学
Research InstitutionKobe University

Principal Investigator

FUKUDA Hideki  Kobe University, Professor, 自然科学研究科, 教授 (30263396)

Project Period (FY) 1998 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 1999: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1998: ¥1,600,000 (Direct Cost: ¥1,600,000)
KeywordsPhospholipase D / Fungus / Recombinant microorganism / Enzyme reaction / 膜内ホスホリパーゼD / バイオ生産物の粘製 / 遺伝子のクローニング / バイオ生産物の精製
Research Abstract

Phospholipase D (PLD1), secreted into the culture medium of Streptoverticillium cinnnamoneum, has been purified to homogeneity and characterized. The Stv.PLD efficiently catalyzes both hydrolysis and transphosphatidylation of various phospholipids, including phosphatidylethanolamine (PE), phosphatidylcholinw (PC), and phosphatidylserine (PS). However, the substrate specificity differs between the two reactions ; PE serves as the most preferred substrate for the hydrolysis, but PC and PS are better substrates than PE for the transphosphatidylation. In addition, the transphosphatidylation but not the hydrolysis of PE and PC is markedly activated on the addition of metal ions, especially ALィイD13ィエD1ィイD2+ィエD2. Nucleotide and amino acid sequence determination of the Stv.PLD revealed the presence of common structural motifs identified in all PLD sequences from various species.
The PLD located in the membrane fraction of Stv.(PLD2) is about 35-40-kDa-monomer enzyme, which is different from the secreted into the culture medium and the smallest molecule among the known PLDs. Anti-PLD1 polyclonal antibody did not cross react with PLD2 by Western blotting, suggesting that the overall structure of PLD2 is not similar to that of PLD1. PLD2 preferentially hydrolyzes PE over PC as a substrate. In the presence of ethanol as a donor of polar headgroup, PLD2 could not catalyze the transphosphatidylation reaction and exclusively produced phosphatidic acid. Thus, The enzymatic properties of PLD2 appear to be substantially different from those of PLD1.

Report

(3 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] C. Ogino et al.: "Purification, Characterization, and Sequence Determination of Phospholipase D Secreted by Streptovirticillium Cinnamoneum"Journal of Biochemistry. 125. 263-269 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] C.Ogino et al.: "Purification, Characterization, and Sequence of Determination of Phospholipase D Secreted by Streptoverticillium cinnnamoneum"Journal of Biochemistry. Vol.125. 263-269 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] C.Ogino et al.: "Purification,Characterization,and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum"Journal of Biochemistry. 125(2). 263-269 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] Ogino,T.et al.: "Purification,Characterization,and Sequence Determination of Phospholipase D Secreted by Streptoverticillium cinnamoneum" Journal of Biochemistry. 125(2). 263-269 (1999)

    • Related Report
      1998 Annual Research Report

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Published: 1998-04-01   Modified: 2016-04-21  

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