|
type |
Journal Article |
authors |
Morozova EA, Kulikova VV, Yashin DV, Anufrieva NV, Anisimova NY, Revtovich SV, Kotlov MI, Belyi YF, Pokrovsky VS, Demidkina TV |
title |
Kinetic Parameters and Cytotoxic Activity of Recombinant Methionine γ-Lyase from Clostridium tetani, Clostridium sporogenes, Porphyromonas gingivalis and Citrobacter freundii |
journal |
Acta Naturae |
Activity |
4.4.1.11 |
Family |
4.4.1.11 |
sel |
selected |
ui |
24303205 |
year |
(2013) |
volume |
5 |
number |
3 |
pages |
92-8 |
| |
keywords |
cytotoxicity; kinetic parameters; methionine γ-lyase; oligomeric structure; pathogenic microorganisms |
abstract |
The steady-state kinetic parameters of pyridoxal 5'-phosphate-dependent recombinant methionine γ -lyase from three pathogenic bacteria, Clostridium tetani, Clostridium sporogenes, and Porphyromonas gingivalis, were determined in β- and γ-elimination reactions. The enzyme from C. sporogenes is characterized by the highest catalytic efficiency in the γ-elimination reaction of L-methionine. It was demonstrated that the enzyme from these three sources exists as a tetramer. The N-terminal poly-histidine fragment of three recombinant enzymes influences their catalytic activity and facilitates the aggregation of monomers to yield dimeric forms under denaturing conditions. The cytotoxicity of methionine γ-lyase from C. sporogenes and C. tetani in comparison with Citrobacter freundii was evaluated using K562, PC-3, LnCap, MCF7, SKOV-3, and L5178y tumor cell lines. K562 (IC50=0.4-1.3 U/ml), PC-3 (IC50=0.1-0.4 U/ml), and MCF7 (IC50=0.04-3.2 U/ml) turned out to be the most sensitive cell lines. |
last changed |
2017/10/02 10:01 |
|