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Title |
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Evolutionary trace analysis at the ligand binding site of laccase
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Authors |
Saharuddin Bin Mohamad1, *, Ai Ling Ong2 and Adiratna Mat Ripen3
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Affiliation |
1Institute of Biological Sciences, University of Malaya, 50603 Kuala Lumpur, Malaysia; 2Multimedia University, Jalan Ayer Keroh Lama, 75450 Melaka, Malaysia; 3Institute for Medical Research, Jalan Pahang, 50588 Kuala Lumpur, Malaysia
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saharuddin@um.edu.my; * Corresponding author
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Article Type |
Hypothesis
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Date |
received April 08, 2008; revised April 29, 2008; accepted May 07, 2008; published June 18, 2008
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Abstract |
Laccase belongs to the family of blue multi-copper oxidases and are capable of oxidizing a wide range of aromatic compounds. Laccases have industrial applications in paper pulping or bleaching and hydrocarbon bioremediation as a biocatalyst. We describe the design of a laccase with broader substrate spectrum in bioremediation. The application of evolutionary trace (ET) analysis of laccase at the ligand binding site for optimal design of the enzyme is described. In this attempt, class specific sites from ET analysis were mapped onto known crystal structure of laccase. The analysis revealed 162PHE as a critical residue in structure function relationship studies.
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Keywords |
evolutionary trace (ET) analysis; laccase; ligand binding site; enzyme bioremediation
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Citation |
Mohamad et al., Bioinformation 2(9): 369-372 (2008)
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Edited by |
P. Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |