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Abstract

Fungal laccases have been extensively exploited for industrial purposes and there is a wealth of information available regarding their reaction mechanism, biological role and several molecular aspects, including cloning, heterologous expression and transcriptional analyses. Here we present the reconstruction of the fungal laccase loci evolution inferred from the comparative analysis of 48 different sequences. The topology of the phylogenetic trees indicate that a single monophyletic branch exists for fungal laccases and that laccase isozyme genes may have evolved independently, possibly through duplication-divergence events. Laccases are copper-containing enzymes generally identified by the utilization of substituted p-diphenol substrates. Interestingly, our approach permitted the assignment of two copper-containing oxidases, preliminarily catalogued as laccases, to a different evolutionary group, distantly related to the main branch of bona fide laccases.

Multiple Multi-Copper Oxidase Gene Families in Basidiomycetes – What for?

“…2 ). As reported previously for C. cinerea , L. bicolor , and P. ostreatus and from enzymes of other species [30,49,54,94], the data strongly supports that genes were multiple duplicated late in evolution at the level of speciation. In accordance to an origin by recent duplication, genes for closely related laccases tend to cluster together within the genomes of Agaricomycetes [48,51,69,95], i. e. in C. cinerea and P. ostreatus in subtelomeric regions of specific chromosomes [49,96,97].…”

Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

“…Laccase isozymes are compared with respect to sequences, phylogenetic relationship, catalytic properties, and expression regulation. Sequence and evolutionary relationship examinations indicate that modern laccase gene families are derived from duplication-divergence events of a small set of ancestral enzymes (Valderrama et al, 2003; Kilaru et al, 2006a; Courty et al, 2009; Kües and Rühl, 2011; Bao et al, 2013; Wang W. et al, 2015). During natural evolution, the laccase paralogs may diversify in their functions, which is supported by numerous biochemical and expression characterization data (Hoegger et al, 2004, 2006; Pezzella et al, 2013; Fan et al, 2014; Yang et al, 2016b).…”

Laccase production by Coriolopsis caperata RCK2011: Optimization under solid state fermentation by Taguchi DOE methodology

“…Majority of the laccases have been reported from white rot fungi, however, they could be found in some other type of fungi, bacteria and insects2. These enzymes are characterized by their ability to catalyze one-electron oxidation of four reducing-substrate molecules concomitant with four-electron reduction of molecular oxygen to water.…”