In silico study to breaking mystery of bioluminescence protein structure of bacterial luciferase and firefly luciferase

Authors

  • A.R. Abdul . Rachman Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia
  • Noor Azmi Shaharuddin Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia
  • M.K. Sabullah School of Food Science and Nutrition, University Malaysia Sabah, Jalan UMS, 88400, Kota Kinabalu, Sabah, Malaysia.
  • M.Y. Shukor Department of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, UPM 43400 Serdang, Selangor, Malaysia

DOI:

https://doi.org/10.54987/bessm.v2i1.115

Abstract

Bioluminescent proteins such as luciferase or green fluorescent protein become an interesting protein to be studied particularly on its structure, mechanism of light emission in certain wavelength and also its contribution in several applications. This study was conducted to understand more on the luciferase enzymes from bacteria and firefly based on in silico studies of their protein sequences, protein surface and interactions with different substrates. Protein crystal structures of bacterial luciferase and firefly luciferase that been deposited on Protein Data Bank (PDB) were used as model proteins for this study. Computer analysis of luciferase proteins such as pI prediction, multiple sequence alignment and molecular docking with different luciferase substrates (Flavin mononucleotide, L-luciferin, D-luciferin, vargulin, coelectrazine, Dinoflagellate luciferin, Latia luciferin) by using iGEMDOCK docking software had been conducted. Final analysis showed that, the bacterial luciferase prefers flavin mononucleotide and latia luciferin as its substrates and for firefly luciferase, it prefers dinoflagellate luciferin, L-luciferin and D-luciferin as the substrates. Bacterial luciferase and firefly luciferase shared very low protein sequence homology (<30%) although they have similar catalyzing function. Prediction of pI by using ProtParam tool showed that bacterial luciferase and firefly luciferase has pI values of 4.95 and 6.42, respectively. In conclusion, bacterial and firefly luciferase can consider several different of luciferin in enzyme catalysis.

Published

2014-07-30

How to Cite

Rachman, A. A. ., Shaharuddin, N. A., Sabullah, M., & Shukor, M. (2014). In silico study to breaking mystery of bioluminescence protein structure of bacterial luciferase and firefly luciferase. Bulletin of Environmental Science and Sustainable Management (e-ISSN 2716-5353), 2(1), 17–23. https://doi.org/10.54987/bessm.v2i1.115

Issue

Vol. 2 No. 1 (2014)

Section

Articles

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