| Literature DB >> 18795108 |
Saharuddin Bin Mohamad1, Ai Ling Ong, Adiratna Mat Ripen.
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.Entities:
Keywords: enzyme bioremediation; evolutionary trace (ET) analysis; laccase; ligand binding site
Year: 2008 PMID: 18795108 PMCID: PMC2533054 DOI: 10.6026/97320630002369
Source DB: PubMed Journal: Bioinformation ISSN: 0973-2063