Evolutionary trace analysis at the ligand binding site of laccase.

Mohamad, S. and Ong, A.L. and Ripen, A.M. (2008) Evolutionary trace analysis at the ligand binding site of laccase. Bioinformation, 2 (9). pp. 369-72. ISSN 0973-2063, DOI 18795108.

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Official URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC253305...


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.

Item Type: Article
Uncontrolled Keywords: Evolutionary trace
Subjects: R Medicine > R Medicine (General)
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Mr. Faizal Hamzah
Date Deposited: 26 Apr 2011 02:56
Last Modified: 26 Apr 2011 02:56
URI: http://eprints.um.edu.my/id/eprint/1028

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