大腸菌由来新規NADH依存性ジヒドロピリミジンデヒドロゲナーゼの機能解析  [in Japanese] Functional analysis of a novel NADH-dependent dihydropyrimidine dehydrogenase from Escherichia coli  [in Japanese]

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Author(s)

Abstract

Dihydropyrimidine dehydrogenase (DPD) is the first and rate-limiting enzyme of the pyrimidine reductive pathway in mammals and plants, and catalyzes the NADPH-dependent reduction of pyrimidines to 5,6-dihydropyrimidines. Although DPD homologs occur in many bacteria, their functions have not been clarified. We purified and characterized novel NADH-dependent DPD, PreT-PreA, from Escherichia coli K12 and NADPH-dependent DPD, PydX-PydA, from Pseudomonas putida. Biochemical and genetic studies revealed that PydX-PydA is the first enzyme of the pyrimidine reductive pathway in P. putida, but PreT-PreA is not involved in the reductive pathway in E. coli, suggesting PreT-PreA represents a novel class of DPDs.

Journal

  • VITAMINS

    VITAMINS 83(9), 528-532, 2009

    THE VITAMIN SOCIETY OF JAPAN

References:  14

Codes

  • NII Article ID (NAID)
    110007387826
  • NII NACSIS-CAT ID (NCID)
    AN00207833
  • Text Lang
    JPN
  • Article Type
    REV
  • ISSN
    0006-386X
  • NDL Article ID
    10443840
  • NDL Source Classification
    ZS8(科学技術--医学--解剖学・生理学・生化学)
  • NDL Call No.
    Z19-36
  • Data Source
    CJP  NDL  NII-ELS  J-STAGE 
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