Molecular analysis of a laccase gene from the white rot fungus Pycnoporus cinnabarinus
Article Abstract:
A laccase-encoding gene (lcc3-1) expressed by Pycnoporus cinnabarinus during growth under xylidine-induced conditions was cloned and structurally analyzed. Its coding region spans more than 2,390 bp, while the corresponding laccase cDNA was identical to the genomic sequence, except for 10 introns 50 to 60 bp in length. A Phe residue was located at a position where it can affect the reduction-oxidation potential of the copper center of the P. cinnabarinus lcc3-1. The P. cinnabarinus lcc3-1 sequence is very similar to the sequence encoding a laccase from Coriolus hirsutus, with the level of similarity placed at 84%.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Novel interaction between laccase and cellobiose dehydrogenase during pigment synthesis in the white rot fungus Pycnoporus cinnabarinus
Article Abstract:
Research was conducted to examine the interaction between laccase and cellobiose dehydrogenase (CDH) during synthesis in the white rot fungus Pycnoporus cinnabarinus. The objectives were to determine whether cinnabarinic acid (CA) levels were dependent on CDH activities, to identify and characterize CDHs and to examine if CDHs control laccase-catalyzed oxidation of 3-hydroxyanthranilic acid to CA. Results indicate that CDHs can regenerate fungal metabolites oxidized by laccase in the presence of a suitable cellulose-derived electron donor.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase
Article Abstract:
Laccase is the major phenoloxidase of the white rot fungus Pycnoporus cinnabarinus. The fungus has no lignin- or manganese-type peroxidases. The addition of 2,5-xylidine increases the production of laccase by a factor of nine. Laccase is a single polypeptide with a molecular weight of about 81,000 Da. Electrophoresis indicates that the enzyme is secreted as a single acidic isoform. Substrate specificity, inhibitor studies and N-terminal amino acid sequence analysis suggests the enzyme is similar to other laccases.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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