Evolutionary and structural diversity of fungal laccases.
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.
Instituto de Biotecnología, Universidad Nacional Autónoma de México, AP 510-3 Cuernavaca, Morelos, Mexico. brenda@ibt.unam.mx
Brenda
B
Valderrama
Patricia
P
Oliver
Arturo
A
Medrano-Soto
Rafael
R
Vazquez-Duhalt
D001665:Binding Sites; D003300:Copper / Q000378:metabolism; D019143:Evolution, Molecular; D005658:Fungi / Q000145:classification / Q000201:enzymology* / Q000235:genetics*; D020440:Gene Duplication; D042845:Laccase / Q000737:chemistry* / Q000235:genetics*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010802:Phylogeny; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D003300:Copper; D042845:Laccase