4-hydroxycinnamoyl-CoA hydratase/lyase (HCHL) - An enzyme of phenylpropanoid chain cleavage from Pseudomonas

Citation
A. Mitra et al., 4-hydroxycinnamoyl-CoA hydratase/lyase (HCHL) - An enzyme of phenylpropanoid chain cleavage from Pseudomonas, ARCH BIOCH, 365(1), 1999, pp. 10-16
Citations number
27
Categorie Soggetti
Biochemistry & Biophysics
Journal title
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
ISSN journal
00039861 → ACNP
Volume
365
Issue
1
Year of publication
1999
Pages
10 - 16
Database
ISI
SICI code
0003-9861(19990501)365:1<10:4H(-AE>2.0.ZU;2-#
Abstract
The enzyme 4-hydroxycinnamoyl-CoA hydratase/lyase (HCHL), which catalyzes a hydration and two-carbon cleavage step in the degradation of 4-hydroxycinn amic acids, has been purified and characterized from Pseudomonas fluorescen s strain AN103. The enzyme is a homodimer and is active with three closely related substrates, 4-coumaroyl-CoA, caffeoyl-CoA, and feruloyl-CoA (K-m va lues: 5.2, 1.6, and 2.4 mu M, respectively), but not with cinnamoyl-CoA or with sinapinoyl-CoA. The abundance of the enzyme reflects a low catalytic c enter activity (2.3 molecules s(-1) at 30 degrees C; 4-coumaroyl-CoA as sub strate). (C) 1999 Academic Press.