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 :
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