STUDI IN SILICO ENZIM GAMMA-LAKTAMASE ARCHAEA Sulfolobus solfataricus: ANALISIS STRUKTURAL DAN FUNGSIONAL
DOI:
https://doi.org/10.31004/jkt.v4i3.16617Keywords:
archaea, in silico, Sulfolobus solfataricus, ?-laktamaseAbstract
Enzim laktamase merupakan salah satu enzim dari archaea, yang diketahui dapat menghambat enzim yang berperan penting dalam virulensi HIV dan Hepatitis B. Enzim tersebut ditemukan pada archaea Sulfolobus solfataricus, dalam 2 jenis, yaitu (+)-Y-laktamase Sso 2810 dan (+)-Y-laktamase 2122. Namun, studi tentang kedua enzim ini belum banyak dilakukan. Penelitian ini bertujuan untuk mengenal lebih lanjut enzim tersebut dengan pendekatan studi in silico. Metode penelitian mencakup penentuan karakteristik fisika protein, analisis struktur primer, sekunder, tersier, beserta analisis fungsi protein. Sekuens enzim diperoleh dalam bentuk FASTA dari NCBI. Selanjutnya analisis dilakukan dengan menggunakan tool seperti ExPASY-ProtParam, SOPMA, RAMPAGE, Swiss Prot Expasy, SIB myhits, InterProScan, TMHMM, dan Peptide Cutter. Hasil identifikasi berdasarkan ExPASY-ProtParam menunjukkan bahwa pI dari enzim ?-laktamase Sso2810 adalah 5,47 dan pI Sso2122 adalah 5,94. Adapun berat molekul dari masing-masing enzim berturut-turut adalah 34950,42 dan 55655,38 pada ?-laktamase Sso2810 dan Sso2212. Nilai indeks alifatik (Sso2810: 101,7) dan (Sso2122:90,14) menyatakan kedua enzim bersifat termostabil. Berdasarkan nilai hidropatisitas, Sso2810 (0,002) bersifat sedikit hidrofobik, sedangkan Ss02122 (-0,197) bersifat hidrofilik. Protein Sso2810 masuk ke dalam famili Acetamidase, sedangkan Sso2122 masuk ke dalam famili Amidase. Berdasarkan hasil studi in silico enzim laktamase Sulfolobus solfataricus tersebut, enzim ini sangat potensial untuk dieksplorasi karakteristiknya lebih jauh sehingga dapat dimanfaatkan secara lebih optimal, salah satunya untuk kandidat anti-HIV dan Hepatitis B.References
Daniel, R.M., Danson, M.J., Hough, D.W., Lee, C.K., Peterson, M.E., and Cowan, D.A. (2008) ‘Enzyme Stability and Activity at High Temperatures’, in ‘Protein Adaptation in Extremophiles’, Siddiqui, K. S. and Thomas, T., Eds., pp. 1–34, Nova Science Publishers, New York, NY, USA
Gao, S., Zhu, S., Huang, R., Li, H., Wang, H., and Zheng, G. (2017) ‘Engineering the Enantioselectivity and Thermostability of a (+)-?-Lactamase from Microbacterium hydrocarbonoxydans for Kinetic Resolution of Vince Lactam (2-Azabicyclo[2.2.1]hept-5-en-3-one)’, Applied and Environmental Microbiology, 84(1), e01780-17.
Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D. and Bairoch, A. (2005) ‘Protein Identification and Analysis Tools on the ExPASy Server’. In: Walker, J.M., Ed., ‘The Proteomics Protocols Handbook’, Humana Press, New York, 571-607.
Ramachandran, G.N., Ramakrishnan, C., and Sasisekharan, V. (1963) ‘Stereochemistry of Polypeptide Chain Configurations’, Journal of Molecular Biology, 7, 95–99.
Reed, C.J., Lewis, H., Trejo, E., Winston, V., and Evilia, C. (2013) ‘Protein Adaptations in Archaeal Extremophiles’, Archaea (Vancouver, B.C.), 2013, 373275.
Taylor, S.J.C., McCague, R., Wisdom, R., Lee, C., Dickson, K., Ruecroft, G., O'Brien, F., Littlechild, J., Bevan, J., Roberts, S.M., and Evans, C.T. (1993) ‘Development of the Biocatalytic Resolution of 2-Azabicyclo[2.2.1]hept-5-en-3-one as an Entry to Single-Enantiomer Carbocyclic Nucleosides’, Tetrahedron: Asymmetry, vol. 4, no. 6, pp. 1117–1128, 1993.
Zhu, S., Huang, R., Gao, S., Li, X., & Zheng, G. (2016). ‘Discovery and Characterization of a Second Extremely Thermostable (+)-?-Lactamase from Sulfolobus solfataricus P2’, Journal of Bioscience and Bioengineering, 121(5), 484–490.
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