4-Hydroxycinnamoyl-CoA Hydratase/lyase (HCHL)ÐAn Enzyme of Phenylpropanoid Chain Cleavage from Pseudomonas
4-Hydroxycinnamoyl-CoA Hydratase/lyase (HCHL)ÐAn Enzyme of Phenylpropanoid Chain Cleavage from Pseudomonas
- Archives of BioChemistry and Biophysics, 365(1), p.10-16, 1999 .
The enzyme 4-hydroxycinnamoyl-CoA hydratase/ lyase (HCHL), which catalyzes a hydration and twocarbon cleavage step in the degradation of 4-hydroxycinnamic acids, has been purified and characterized from Pseudomonas fluorescens strain AN103. The enzyme is a homodimer and is active with three closely related substrates, 4-coumaroyl-CoA, caffeoyl-CoA, and feruloyl-CoA (Km values: 5.2, 1.6, and 2.4 mM, respectively), but not with cinnamoyl-CoA or with sinapinoyl- CoA. The abundance of the enzyme reflects a low catalytic center activity (2.3 molecules s21 at 30°C; 4-coumaroyl-CoA as substrate).
PSEUDOMONAS FLUORESCENS
HYDROXYCINNAMIC ACID
PHENYLPROPANOID
FERULIC ACID
VANILLIN
ENOYL-COA HYDRATASE
The enzyme 4-hydroxycinnamoyl-CoA hydratase/ lyase (HCHL), which catalyzes a hydration and twocarbon cleavage step in the degradation of 4-hydroxycinnamic acids, has been purified and characterized from Pseudomonas fluorescens strain AN103. The enzyme is a homodimer and is active with three closely related substrates, 4-coumaroyl-CoA, caffeoyl-CoA, and feruloyl-CoA (Km values: 5.2, 1.6, and 2.4 mM, respectively), but not with cinnamoyl-CoA or with sinapinoyl- CoA. The abundance of the enzyme reflects a low catalytic center activity (2.3 molecules s21 at 30°C; 4-coumaroyl-CoA as substrate).
PSEUDOMONAS FLUORESCENS
HYDROXYCINNAMIC ACID
PHENYLPROPANOID
FERULIC ACID
VANILLIN
ENOYL-COA HYDRATASE