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