Evolutionary trace analysis at the ligand binding site of laccase

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...

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Detalles Bibliográficos
Autores principales: Mohamad, Saharuddin Bin, Ong, Ai Ling, Ripen, Adiratna Mat
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2008
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2533054/
https://www.ncbi.nlm.nih.gov/pubmed/18795108
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author Mohamad, Saharuddin Bin
Ong, Ai Ling
Ripen, Adiratna Mat
author_facet Mohamad, Saharuddin Bin
Ong, Ai Ling
Ripen, Adiratna Mat
author_sort Mohamad, Saharuddin Bin
collection PubMed
description 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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spelling pubmed-25330542008-09-15 Evolutionary trace analysis at the ligand binding site of laccase Mohamad, Saharuddin Bin Ong, Ai Ling Ripen, Adiratna Mat Bioinformation Hypothesis 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. Biomedical Informatics Publishing Group 2008-06-18 /pmc/articles/PMC2533054/ /pubmed/18795108 Text en © 2008 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Mohamad, Saharuddin Bin
Ong, Ai Ling
Ripen, Adiratna Mat
Evolutionary trace analysis at the ligand binding site of laccase
title Evolutionary trace analysis at the ligand binding site of laccase
title_full Evolutionary trace analysis at the ligand binding site of laccase
title_fullStr Evolutionary trace analysis at the ligand binding site of laccase
title_full_unstemmed Evolutionary trace analysis at the ligand binding site of laccase
title_short Evolutionary trace analysis at the ligand binding site of laccase
title_sort evolutionary trace analysis at the ligand binding site of laccase
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2533054/
https://www.ncbi.nlm.nih.gov/pubmed/18795108
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