放線菌Streptomyces sp. 590由来L-メチオニン脱炭酸酵素の精製および性質検討  [in Japanese] Purification and characterization of L-methionine decarboxylase from Streptomyces sp. 590  [in Japanese]

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Abstract

L-Methionine decarboxylase [EC 4.1.1.57] catalyzes the decarboxylation of L-methionine and is a pyridoxal 5'-phosohate(PLP)-dependent enzyme. L-Methionine decarboxylase has been purified 630-fold by DEAE-Toyopearl 650M, Phenyl-Toyopearl 650M and Sephacryl S-300 column chromatographies from Streptomyces sp.590. The enzyme has a dimeric structure with identical subunits of Mr 60,000. This enzyme shows optimum activity at pH7.0 and 45°C, and is stable between pH5.7 and pH9.0. L-Methionine decarboxylase has antitumor activity against RERF-LC-AI and HeLa cells. Ten N-terminal amino acid sequence of L-methionine decarboxylase was determined, and the sequence showed no homology with other reported proteins.

Journal

  • Scientific Reports of the Faculty of Agriculture, Okayama University

    Scientific Reports of the Faculty of Agriculture, Okayama University 100, 3-7, 2011-02

    岡山大学農学部

Codes

  • NII Article ID (NAID)
    120002828168
  • NII NACSIS-CAT ID (NCID)
    AN00033029
  • Text Lang
    JPN
  • Article Type
    departmental bulletin paper
  • Journal Type
    大学紀要
  • ISSN
    04740254
  • NDL Article ID
    11027497
  • NDL Source Classification
    ZR7(科学技術--農林水産--農産)
  • NDL Call No.
    Z18-436
  • Data Source
    NDL  IR 
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