Jill Angela Wahleithner

TL;DR: It is speculated that structural differences in the substrate-activation site (a 'blue', type 1 copper center) control the redox potential range as well as substrate specificity, and the cystine content contributes to stability.

TL;DR: Although the redox potentials were not significantly altered, the Km, kcat and fluoride inhibition of the laccases were greatly changed by the mutations, interpreted as possible mutation-induced structural perturbations on the molecular recognition between the reducing substrate and laccase and on the electron transfer from the substrate to the type-1 Cu centre.

TL;DR: Four distinct laccase genes have been identified in the fungus Rhizoctonia solani and hybridization analyses indicate that each of the four lacc enzyme genes is present in a single copy in the genome.

TL;DR: Nucleotide sequence analysis shows that Trichoderma harzianum and Penicillium purpurogenum α1,3-glucanases (mutanases) have homologous primary structures, and the catalytic domains and the binding domains were assigned to a new family of glycoside hydrolases and to anew family of carbohydrate-binding domains, respectively.

TL;DR: In this paper, isolated nucleic acid fragments containing a sequence encoding a Rhizoctonia solani laccase having optimum activity at a neutral or basic pH, and the encoded proteins encoded thereby.