2005
DOI: 10.1016/j.enzmictec.2004.03.022
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LAC3, a new low redox potential laccase from Trametes sp. strain C30 obtained as a recombinant protein in yeast

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Cited by 69 publications
(68 citation statements)
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References 38 publications
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“…= 2.04) and for the T2 (g k = 2.25; A k = 162 G), similar to those for LAC3 and other laccases reported previously. [7,8] After approximately 25 min of irradiation the sample was ESR-silent, which indicated that both the T1 and T2 coppers were reduced. This formally indicates that at least two electrons were transferred to the enzyme.…”
mentioning
confidence: 99%
See 1 more Smart Citation
“…= 2.04) and for the T2 (g k = 2.25; A k = 162 G), similar to those for LAC3 and other laccases reported previously. [7,8] After approximately 25 min of irradiation the sample was ESR-silent, which indicated that both the T1 and T2 coppers were reduced. This formally indicates that at least two electrons were transferred to the enzyme.…”
mentioning
confidence: 99%
“…C30 [7] ), which ultimately converts dioxygen into water by using ruthenium(II) polypyridine-type chromophores (complexes 1 and 2, Scheme 1) and ethylenediaminetetraacetic acid (EDTA) as the sacrificial electron donor.…”
mentioning
confidence: 99%
“…[9,10] It contains as urface-located type 1c opper (T1, substrate oxidation center) connected to at rinuclear center (dioxygen reduction center) structuredb etween at ype 3p air of anti-ferromagnetically coupled copper ions (T3) and at ype 2c opperi on (T2). [11] It oxidizes aw ide range of substrates (e.g.,p henols, aromatic amines,m etal ions) under slightly acidic conditions and is stable for days at ambient temperatures.…”
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confidence: 99%
“…The inability of yeasts to process different laccases post-translationally with the same efficiency may influence the observed "selectivity" in expression. 76 Laccase expression in yeasts has been investigated taking into account an array of different parameters with controversial results. For instance, both native laccase or yeast signal peptides (S. cerevisiae α-factor or invertase; K. lactis killer toxin; Y. lipolytica XPR2) have been used with different results for various expressed enzymes.…”
Section: Yeast Recombinant Systemsmentioning
confidence: 99%
“…113 Furthermore, heterologous expression has been often used as a strategy to get around the problem of obtaining laccase isoforms not easily producible in natural hosts. 66,76,84,86,87,93 Some other authors have reported the production of recombinant laccases as a model (1) to better understand copper trafficking and the hierarchy of copper distribution in the cell; 73 (2) to examine the protein quality control mechanism; 83 (3) to study the induction of its own promoter by oxidative stress; 85 (4) to explore the possible use of hypoxic induction of the KlPDC1 promoter to direct heterologous gene expression in yeasts. 111 Development of applications of recombinant laccases from yeasts is discussed in a next section.…”
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confidence: 99%