Preview

Proceedings of the National Academy of Sciences of Belarus, Chemical Series

Advanced search

COMPARATIVE ANALYSIS OF M. TUBERCULOSIS CYP124 REDUCTION WITH DIFFERENT REDOX PARTNERS

https://doi.org/10.29235/1561-8331-2018-54-2-190-196

Abstract

In order to determine the optimal redox partners of CYP124 M. tuberculosis in reconstituted in vitro system we carried out heterologous expression, isolation and purification of recombinant CYP124 Mycobacterium tuberculosis and candidate redox partners: Fdx, FdR, FprA, Adx, AdR, CPR, Arh1_A18G, Etpfd. CYP124 was shown to exhibit the highest catalytic activity in system with S. pombe mitochondrial electron transfer proteins: Etp1fd и Arh1_A18G.

About the Authors

A. M. Tumilovich
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Anastasiya M. Tumilovich – Researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



A. A. Kavaleuski
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Anton A. Kavaleuski – Junior researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



T. S. Varaksa
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Tatsiana S. Varaksa – Junior researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



A. V. Vasilevskaya
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Anna V. Vasilevskaya – Ph. D. (Chemistry), Senior researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



T. S. Cherkesova
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Tatsiana S. Cherkesova – Researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



I. P. Grabovets
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Irina P. Grabovets – Researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



T. V. Shkel
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Tatsiana V. Shkel – Researcher.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



Ya. V. Dichenko
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Yaroslav V. Dichenko – Senior researcer.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



A. A. Gilep
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus.
Belarus

Andrei A. Gilep – Ph. D. (Chemistry), Head of the Laboratory.

5/2, Acad. V. F. Kuprevich Str., 220141, Minsk.



References

1. Vasilevskaya A. V., Sergeev G. V., Gilep A. A., Usanov S. A. Structure analysis of cytochromes P450 of Mycobacterium tuberculosis complex mycobacteria. Doklady Natsionalnoi Akademii Nauk Belarusi = Doklady of the National Academy of Sciences of Belarus, 2010, vol. 54, no. 5, pp. 55–59 (in Russian).

2. Vasilevskaya A .V., Yantsevich A. V., Sergeev G. V., Lemish A. P., Usanov S. A., Gilep A. A. Identification of Mycobacterium tuberculosis enzyme involved in vitamin D and 7-dehydrocholesterol metabolism. The Journal of Steroid Bioche- mistry and Molecular Biology, 2017, vol. 169, pp. 202–209. DOI: 10.1016/j.jsbmb.2016.05.021

3. Ewen K. M., Schiffler B., Uhlmann-Schiffler H., Bernhardt R., Hannemann F. The endogenous adrenodoxin reductase-like flavoprotein arh1 supports heterologous cytochrome P450-dependent substrate conversions in Schizosaccharomyces pombe. FEMS Yeast Res, 2008, vol. 8, no. 3. – P. 432–441. DOI: 10.1111/j.1567-1364.2008.00360.x

4. Müller J. J., Hannemann F., Schiffler B., Ewen K. M., Kappl R., Heinemann U., Bernhardt R. Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe. Journal of Inorganic Biochemistry, 2011, vol. 105, no. 7, pp. 957-965. DOI: 10.1016/j.jinorgbio.2011.04.001

5. Vasilevskaya A. V., Rusak A. A., Sergeev G.V., Gilep A. A., Usanov S. A. Mycobacterium tuberculosis cytochrome P450124: ligand-binding and catalytic properties. Vestsі Nacyyanal’naj akademіі navuk Belarusі. Seryya khіmіchnykh navuk = Proceedings of the National Academy of Sciences of Belarus. Chemical Series, 2011, no. 3, pp 107–112 (in Russian).

6. Strushkevich N., MacKenzie F., Cherkesova T., Grabovec I., Usanov S., Park H. W. Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proceedings of the National Academy of Sciences, 2011, vol. 108, no. 25, pp. 10139–10143. DOI: 10.1073/pnas.1019441108

7. Bonina T. A., Gilep A. A., Estabrook R. W., Usanov S. A. Engineering of proteolytically stable NADPH-cytochrome P450 reductase. Biochemistry (Moscow), 2005, vol. 70, no. 3, pp. 357-365. DOI: 10.1007/s10541-005-0122-3

8. Novagen. pET System Manual. 11th Ed. Darmstadt, EMD Biosciences, Inc., 2005. 80 p.

9. Bellamine A., Mangla A. T., Nes W. D., Waterman M. R. Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis. Proceedings of the National Academy of Sciences, 1999, vol. 96, no. 16, pp. 8937-8942. DOI: 10.1073/pnas.96.16.8937

10. Fischer F., Raimondi D., Aliverti A., Zanetti G. Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase. European Journal of Biochemistry, 2002, vol. 269, no. 12, pp. 3005–3013. DOI: 10.1046/j.1432-1033.2002.02989.x

11. Murataliev M. B., Feyereisen R., Walker F. A. Electron transfer by diflavin reductases. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics, 2004, vol. 1698, no. 1, pp. 1–26. DOI: 10.1016/j.bbapap.2003.10.003


Review

Views: 781


Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.


ISSN 1561-8331 (Print)
ISSN 2524-2342 (Online)