2011
DOI: 10.1107/s1744309111021129
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Purification, crystallization and preliminary X-ray structure analysis of the laccase fromGanoderma lucidum

Abstract: The ligninolytic enzymes of the basidiomycetes play a key role in the global carbon cycle. A characteristic property of these enzymes is their broad substrate specificity, which has led to their use in various biotechnologies, thus stimulating research into the three-dimensional structures of ligninolytic enzymes. This paper presents the purification, crystallization and preliminary X-ray analysis of the laccase from the ligninolytic basidiomycete Ganoderma lucidum.

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Cited by 6 publications
(6 citation statements)
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“…Laccases are copper-containing polyphenol oxidases and are homologous with ascorbate oxidase and with mammalian plasma protein ceruloplasmin, which belong to the blue multi-copper oxidase family and have several similarities in structure and functionality 1 . Laccases play vital roles in the natural carbon cycle and facilitate direct reduction of molecular oxygen to water 2 . Even in the absence of H 2 O 2 and of other secondary metabolites, the substrate may be directly oxidized by laccases as long as dissolved oxygen exists 3 .…”
Section: Introductionmentioning
confidence: 99%
“…Laccases are copper-containing polyphenol oxidases and are homologous with ascorbate oxidase and with mammalian plasma protein ceruloplasmin, which belong to the blue multi-copper oxidase family and have several similarities in structure and functionality 1 . Laccases play vital roles in the natural carbon cycle and facilitate direct reduction of molecular oxygen to water 2 . Even in the absence of H 2 O 2 and of other secondary metabolites, the substrate may be directly oxidized by laccases as long as dissolved oxygen exists 3 .…”
Section: Introductionmentioning
confidence: 99%
“…Except for these, LZ-8, a protein isolated from G. lucidum mycelia, has been shown to have immunomodulating activity [12] , [24] , and its structural, biochemical and immunological properties have been studied in much detail [25] – [28] . Moreover, numerous laccase isozymes which have ligninolytic capabilities have also been identified from G. lucidum [6] , [7] , [29] .…”
Section: Introductionmentioning
confidence: 99%
“…The molecular structures of laccases have been reported by several groups. Briozzo et al and Piotek et al independently first succeeded in determining the structure of a laccase from Trametes versicolor . , A visible representation of the structure of this enzyme is shown in Figure . This laccase can be divided into three domains and has four copper ions, and the T1 copper ion locates in domain 3, and the trinuclear copper cluster (T2, T3a, and T3b) is embedded between domains 1 and 3 (Figure ).…”
Section: Introductionmentioning
confidence: 99%
“…Since then, numerous papers have been published on this unique enzyme; 12 952 references are currently listed for the topic of “laccase*” in the database of the Web of Science Core Collections (September 17, 2020). Laccases are now used in many fields of biotechnology such as biopulping, textile dye bleaching, bioremediation, biological fuel cells, and biosensors. Laccases belong to the blue-copper family of oxidases that mediate the oxidative degradation or polymerization of polyphenol formation in plants by inducing the radical polymerization of polyphenol derivatives; thus, laccases are widely found in plants, fungi, bacteria, and insects. …”
Section: Introductionmentioning
confidence: 99%