KINETIC PARAMETERS AND CYTOTOXIC ACTIVITY OF RECOMBINANT METHIONINE γ-LYASE FROM CLOSTRIDIUM TETANI, CLOSTRIDIUM SPOROGENES, PORPHYROMONAS GINGIVALIS AND CITROBACTER FREUNDII
| Autor: | N. Y. Anisimova, Tatyana V. Demidkina, D. V. Yashin, Vadim S. Pokrovsky, Elena A. Morozova, S.V. Revtovich, Yury Belyi, Natalya V. Anufrieva, M. I. Kotlov, Vitalia V. Kulikova |
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| Jazyk: | ruština |
| Rok vydání: | 2013 |
| Předmět: |
Clostridium tetani
Clostridium sporogenes oligomeric structure Biology medicine.disease_cause Biochemistry law.invention chemistry.chemical_compound law medicine METHIONINE γ-LYASE Molecular Biology Porphyromonas gingivalis pathogenic microorganisms chemistry.chemical_classification Methionine kinetic parameters Lyase biology.organism_classification Citrobacter freundii Enzyme chemistry Recombinant DNA cytotoxicity Molecular Medicine Research Article Biotechnology |
| Zdroj: | Scopus-Elsevier Acta Naturae |
| ISSN: | 2075-8251 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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