Anticancer Enzyme L-Lysine α-Oxidase: Properties and Application Perspectives
| Autor: | Galina K. Guerassimova, Galina A. Firsova, Temir T. Berezov, Ludmila A. Sedakova, Helena M. Treshalina, Elena V. Lukasheva, Natalia V. Gogichaeva |
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| Rok vydání: | 2000 |
| Předmět: |
chemistry.chemical_classification
Oxidase test Bioengineering Oxidative deamination Biological activity General Medicine Biology L-amino-acid oxidase Applied Microbiology and Biotechnology Biochemistry Molecular biology Mechanism of action chemistry Oxidoreductase In vivo medicine medicine.symptom Molecular Biology L-lysine oxidase Biotechnology |
| Zdroj: | Applied Biochemistry and Biotechnology. 88:267-274 |
| ISSN: | 0273-2289 |
| DOI: | 10.1385/abab:88:1-3:267 |
| Popis: | Fungal L-lysine α-oxidase (1.4.3.14) (LO) from Trichodermaharzianum Rifai presents an oxidoreductase with a firmly attached coenzyme—FAD. This stable enzyme catalyzes an oxidative deamination of L-lysine yielding hydrogen peroxide, ammonia, and α-ketoacid. LO exhibits antitumor activity toward 5 of 12 tested transplantable tumors. The sensitive tumors were ascitichepatoma 22 (T/C=201%, CR=66%); mammary adenocarcinoma Ca-755 (TGI=96%); melanoma B-16 (TGI=81%); AKATOL (TGI=75%); RSHM 5 (TGI=79%). LO therapeutic activity was observed within a wide range of doses, 35–350 U/kg, by intraperitoneal daily injections for 5 d. Contrary to Escherichia coli L-asparaginase, LO demonstrates its antitumor activity by the low therapeutic doses in vivo within a wide range of optimal doses and through an other antitumor spectrum. Fisher lymphadenosis L-5178y highly sensitive toward L-asparaginase appeared to be LO resistant. The possible mechanisms of LO antitumor activity through the key biochemical processes are discussed. |
| Databáze: | OpenAIRE |
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