Author:
Morozova E. A.,Kulikova V. V.,Yashin D. V.,Anufrieva N. V.,Anisimova N. Y.,Revtovich S. V.,Kotlov M. I.,Belyi Y. F.,Pokrovsky V. S.,Demidkina T. V.
Abstract
The steady-state kinetic parameters of pyridoxal 5-phosphate-dependent recombinant methionine -lyase from three pathogenic bacteria, Clostridium tetani, Clostridium sporogenes, and Porphyromonas gingivalis, were determined in - and -elimination reactions. The enzyme from C. sporogenes is characterized by the highest catalytic efficiency in the -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 -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.
Subject
Molecular Biology,Molecular Medicine,Biochemistry,Biotechnology
Cited by
27 articles.
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