Enzymatic alteration in the shikimate pathway during derivation of menaquinone-4-producing mutants of Flavobacterium sp. 238-7.

  • TAGUCHI Hisataka
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
  • KITA Shunbun
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
  • TANI Yoshiki
    Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University

この論文をさがす

抄録

Activities of seven enzymes of the shikimate pathway were compared between the wild-type strain and menaquinone-4-producing mutant strains of Flavobacterium sp. 238-7. Activity of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) synthase, the first regulatory enzyme in the shikimate pathway, was almost the same in these strains in the stationary phase, but the activity of a sulfonamide-resistant strain, SP0736, was 2 times higher than that of other strains in the logarithmic phase. Shikimate dehydrogenase activity was almost the same among these strains during cultivation. Other enzyme activities of mutants were 1.5-4 fold higher than those of the wild-type strain. DAHP synthase and shikimate kinase were found to be inhibited by chorismate and MK-4. Feedback inhibition for shikimate kinase by chorismate was partially removed in strain SP0736.

収録刊行物

被引用文献 (1)*注記

もっと見る

詳細情報

  • CRID
    1390282681441794432
  • NII論文ID
    110006325431
  • NII書誌ID
    AA00515312
  • DOI
    10.1271/bbb1961.55.769
  • ISSN
    18811280
    00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

問題の指摘

ページトップへ