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B6db references: 84154841

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
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

B6db references