type	Journal Article
authors	Demidkina, T. V.; Miagkikh, I. V.; Faleev, N. G.; Belikov, V. M.
title	[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius]
journal	Biokhimiia
Activity	4.1.99.2
ui	84154841
year	(1984)
volume	49
number	1
pages	32-7.
keywords	Ammonium Compounds/pharmacology
abstract	A method for preparation of homogeneous tyrosine phenol lyase (EC 4.199.2) from Citrobacter intermedius has been developed. The cells were cultivated in the media with a view to obtain a cell culture with a high activity of tyrosine phenol lyase. The isoelectric point for the enzyme lies at pH 4.9. Tyrosine phenol lyase is strictly stereospecific: it catalyzes the formation of pyruvate only from L- tyrosine, but not from D-tyrosine. Kinetic studies showed that K+ and NH4+ cations are non-competitive activators of the enzyme (Ka = 3.57 X 10(-3) and 1.34 X 10(-4) M, respectively).
last changed	2002/11/12 16:17