Molecular and Catalytic Properties of Monoacetylphloroglucinol Acetyltransferase from Pseudomonas sp. YGJ3

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Monoacetylphloroglucinol (MAPG) acetyltransferase, catalyzing the conversion of MAPG to 2,4-diacetylphloroglucinol (DAPG), was purified from <I>Pseudomonas</I> sp. YGJ3 grown without Cl<SUP>−</SUP>. Cl<SUP>−</SUP> and pyoluteorin repressed expression of the enzyme. SDS-polyacrylamide gel electrophoresis showed that the purified enzyme (<I>M</I><SUB>r</SUB>=330 kDa) was composed of three subunits of 17, 38, and 43 kDa, and protein sequencing identified these as PhlB, PhlA, and PhlC respectively. The enzyme catalyzed the reversible disproportionation of 2 moles of MAPG to phloroglucinol (PG) and DAPG. The equilibrium constant <I>K</I> (=[DAPG][PG]/[MAPG]<SUP>2</SUP>) was estimated to be about 1.0 at 25 °C. A <I>Kpn</I>I 20-kb DNA fragment was cloned from the genomic DNA of strain YGJ3, and a 12,598-bp long DNA region containing the <I>phl</I> gene cluster <I>phlACBDEFGHI</I> was sequenced. PCR cloning and expression of the <I>phl</I> genes in <I>Escherichia coli</I> confirmed that expression of <I>phlACB</I> genes produced MAPG ATase.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 76(3), 559-566, 2012-03-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10030750830
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    023553862
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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