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245	1	0	_a4-Hydroxycinnamoyl-CoA Hydratase/lyase (HCHL)ÐAn Enzyme of Phenylpropanoid Chain Cleavage from Pseudomonas
490	0		_vArchives of BioChemistry and Biophysics, 365(1), p.10-16, 1999
520	3		_aThe 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).
650	1	4	_aPSEUDOMONAS FLUORESCENS
650	1	4	_aHYDROXYCINNAMIC ACID
650	1	4	_aPHENYLPROPANOID
650	1	4	_aFERULIC ACID
650	1	4	_aVANILLIN
650	1	4	_aENOYL-COA HYDRATASE
700	1	2	_aMitra, A.
700	1	2	_aKitamura, Y.
700	1	2	_aGasson, M.J.
700	1	2	_aNarbad, A.
700	1	2	_aParr, A.J.
700	1	2	_aPayne, J.
700	1	2	_aRhodes, M.J.C.
700	1	2	_aRhodes, M.J.C.
700	1	2	_aWalton, N.J.
856	4	0	_uhttps://drive.google.com/file/d/1kFdlXXGItDxo2e7WJP0VFCFnh8vcSVsu/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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