Metabolism of 1-aminocyclopropane-1-carboxylic acid.

抄録

Several microorganisms capable of utilizing 1-aminocyclopropane-l-carboxylate (ACPC) were isolated from soil. A bacterium which belongs to Pseudomonas accumulated cellular a-aminobutyrate with consumption of ACPC and cells incubated with ACPC medium had the activity deaminating the substrate to form α-ketobutyrate. An enzyme, ACPC deaminase, was highly purified and its molecular weight, substrate specificity and absorption spectrum were investigated. These results suggested that this enzyme was a pyridoxal 5'-phosphate enzyme which has the molecular weight of 104000 and high specificity for ACPC, Km=1.5mM. A yeast, Hansenula saturnus, is also capable of forming ACPC deaminase, which has a lower molecular weight, 69000, and higher Km value, 2.6mM.

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詳細情報 詳細情報について

  • CRID
    1390001206468574336
  • NII論文ID
    130003525829
  • DOI
    10.1271/bbb1961.42.1825
  • COI
    1:CAS:528:DyaE1MXhtFKru7k%3D
  • 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

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