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.
Highlights
White rot fungus such as Trametes versicolor is a good candidate for biodegradation of aromatic compound in soil
Laccase from Trametes versicolor has been reported to be involved in degradation
The trace status of amino acid residues at the Laccase from Trametes versicolor was used as seed ligand binding site is given in Table 1
Summary
White rot fungus such as Trametes versicolor is a good candidate for biodegradation of aromatic compound in soil. This method relies on both sequence and structural information to analyze functional sites of a protein or group of proteins It identifies the conserved amino acid residues in an alignment and maps the information onto known 3D protein structures. We defined the ligand binding site in 1KYA as the Consensus sequences derived from the entire cutoff amino acid residues within 5Å distance from the ligand, partitions were aligned and compared with the amino. The trace status of amino acid residues at the Laccase from Trametes versicolor was used as seed ligand binding site is given in Table 1 (supplementary sequence in our analysis because it was reported as an material). All of the trace residues that are forms hydrogen bonding with the ligand and coordinates neutral at the binding site are non-polar amino acid the copper C1 atom that functions as the primary (162Phe, 164Leu, 265Phe, 332Phe, 337Phe and 391Pro). They vary in length from 517 to 533 residues binding cavity for the entry of larger substrates
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