title: Evolutionary trace analysis at the ligand binding site of laccase.
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.
authors.affiliation: Institute of Biological Sciences, University of Malaya, 50603 Kuala Lumpur, Malaysia. saharuddin@um.edu.my
authors.forename: Saharuddin Bin
authors.initials: SB
authors.lastname: Mohamad
authors.forename: Ai Ling
authors.initials: AL
authors.lastname: Ong
authors.forename: Adiratna Mat
authors.initials: AM
authors.lastname: Ripen
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