Abstract
Genome analyses revealed in various basidiomycetes the existence of multiple genes for blue multi-copper oxidases (MCOs). Whole genomes are now available from saprotrophs, white rot and brown rot species, plant and animal pathogens and ectomycorrhizal species. Total numbers (from 1 to 17) and types of mco genes differ between analyzed species with no easy to recognize connection of gene distribution to fungal life styles. Types of mco genes might be present in one and absent in another fungus. Distinct types of genes have been multiplied at speciation in different organisms. Phylogenetic analysis defined different subfamilies of laccases sensu stricto (specific to Agaricomycetes), classical Fe2+-oxidizing Fet3-like ferroxidases, potential ferroxidases/laccases exhibiting either one or both of these enzymatic functions, enzymes clustering with pigment MCOs and putative ascorbate oxidases. Biochemically best described are laccases sensu stricto due to their proposed roles in degradation of wood, straw and plant litter and due to the large interest in these enzymes in biotechnology. However, biological functions of laccases and other MCOs are generally little addressed. Functions in substrate degradation, symbiontic and pathogenic intercations, development, pigmentation and copper homeostasis have been put forward. Evidences for biological functions are in most instances rather circumstantial by correlations of expression. Multiple factors impede research on biological functions such as difficulties of defining suitable biological systems for molecular research, the broad and overlapping substrate spectrum multi-copper oxidases usually possess, the low existent knowledge on their natural substrates, difficulties imposed by low expression or expression of multiple enzymes, and difficulties in expressing enzymes heterologously.
Highlights
The milky sap (Urushi juice) of the lacquer tree Rhus vernicifera hardens in the presence of air
Phylogenetic analysis defined different subfamilies of laccases sensu stricto, classical Fe2+-oxidizing Fet3-like ferroxidases, potential ferroxidases/laccases exhibiting either one or both of these enzymatic functions, enzymes clustering with pigment multi-copper oxidases (MCOs) and putative ascorbate oxidases
Fungal laccases are suggested to act in lignocellulose degradation [18,19], in soil organic matter cycling and in ectomycorrhizal life style [20,21], in fruiting body formation [22], in different pathways of pigment production [23,24], in fungal plant-pathogen interaction [23,24] and defense [25,26], and in stress response on diverse environmental challenges [23,27] but details on the mode of actions remain unknown
Summary
The milky sap (Urushi juice) of the lacquer tree Rhus vernicifera hardens in the presence of air. Since ancient times, this principle has been made use of in artwork in the form of lustrous translucent varnish under addition of suitable pigments, first in China and later in Japan and other Asian countries [1]. Much work is driven by the high interest in laccases in biotechnology – the enzymes have multiple applications in textile industries and dye decolorization [6,7], food industries [8], wood products industries [9], paper pulp bleaching [10], bioremediation [11], biofuel cells [12], biosensor applications [13], and others [14,15,16]. Laccases (EC 1.10.3.2; synonyms: urishiol or urushiol oxidase, p-diphenol oxidase, p-diphenol oxidase:dioxygen oxidoreductase, benzenediol:oxygen oxidoreductase) act with low specificity on both o- and Multiple Multi-Copper Oxidase Genes in Basidiomycetes
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