In Silico Generation of Laccase Mutants from Lacc 6 of Pleurotus ostreatus and Bacterial Enzymes.
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Date
2018-03-15Author
Díaz, Rubén
Mercado Flores, Yuridia
Díaz Godínez, Gerardo
Herrera Zúñiga, Leonardo David
Álvarez Cervantes, Jorge
Anducho Reyes, Miguel Angel
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In this research, 63 complete amino acid sequences of laccase enzymes
from fungi (40), bacteria (5), insects (8), and plants (10) were used for a
phylogenetic analysis. A common ancestor that diverged in the laccases
in prokaryote and eukaryote was observed. Additionally, it was determined
that there was a difference in the type of amino acids bound to the
histidines linked to the copper atoms of the active site, and that a fungal
laccase of approximately 279 Ma was an ancestor of the laccases in the
basidiomycetes considered in this study. In contrast, Lacc 6 of Pleurotus
ostreatus was used as a template to generate mutants. Through modeling,
the changes in the secondary and tertiary structures of this enzyme were
observed with the substitution of amino acids adjacent to histidines in the
conserved region of the active site, via the presence of amino acids in a
similar place in the laccases of bacteria.