• Title of article

    4-Hydroxycinnamoyl-CoA Hydratase/lyase (HCHL)—An Enzyme of Phenylpropanoid Chain Cleavage fromPseudomonas

  • Author/Authors

    Mitra، نويسنده , , Adinpunya and Kitamura، نويسنده , , Yoshie and Gasson، نويسنده , , Michael J and Narbad، نويسنده , , Arjan and Parr، نويسنده , , Adrian J and Payne، نويسنده , , John and Rhodes، نويسنده , , Michael J.C and Sewter، نويسنده , , Ciaran and Walton، نويسنده , , Nicholas J، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 1999
  • Pages
    7
  • From page
    10
  • To page
    16
  • Abstract
    The enzyme 4-hydroxycinnamoyl-CoA hydratase/lyase (HCHL), which catalyzes a hydration and two-carbon cleavage step in the degradation of 4-hydroxycinnamic acids, has been purified and characterized fromPseudomonas fluorescensstrain AN103. The enzyme is a homodimer and is active with three closely related substrates, 4-coumaroyl-CoA, caffeoyl-CoA, and feruloyl-CoA (Kmvalues: 5.2, 1.6, and 2.4 μM, respectively), but not with cinnamoyl-CoA or with sinapinoyl-CoA. The abundance of the enzyme reflects a low catalytic center activity (2.3 molecules s−1at 30°C; 4-coumaroyl-CoA as substrate).
  • Keywords
    Pseudomonas Fluorescens , Hydroxycinnamic acid , phenylpropanoid , ferulic acid , vanillin , enoyl-CoA hydratase
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    1999
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1614449

    • Link To Document
    https://search.isc.ac/dl/search/defaultta.aspx?DTC=10&DC=1614449