|
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 |
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