A homodimeric laccase with unique characteristics from the yellow mushroom Cantharellus cibarius

Ng, Tzi Bun; Wang, H.X

doi:10.1016/j.bbrc.2003.11.087

Cited by 69 publications

(40 citation statements)

References 33 publications

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“…Considering that most laccases have been found in fungi and plants, some eukaryotes may also contain TdMCBPs. Recently, a homodimeric protein with laccase activity was isolated from yellow mushroom (Cantharellus cibarius) [128]. The molecular weight of this enzyme as a monomer was 46 kDa.…”

Section: Small Laccases In Fungismentioning

confidence: 99%

Function and molecular evolution of multicopper blue proteins

Nakamura

Gō

2005

Cell. Mol. Life Sci.

242

140

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Multicopper blue proteins (MCBPs) are multidomain proteins that utilize the distinctive redox ability of copper ions. There are a variety of MCBPs that have been roughly classified into three different groups, based on their domain organization and functions: (i) nitrite reductase-type with two domains, (ii) laccase-type with three domains, and (iii) ceruloplasmin-type with six domains. Together, the second and third group are often commonly called multicopper oxidases (MCOs). The rapid accumulation of genome sequence information in recent years has revealed several new types of proteins containing MCBP domains, mainly from bacteria. In this review, the recent research on the functions and structures of MCBPs is summarized, mainly focusing on the new types. The latter half of this review focusses on the two domain MCBPs, which we propose as the evolutionary intermediate of the MCBP family.

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Section: Small Laccases In Fungismentioning

confidence: 99%

Function and molecular evolution of multicopper blue proteins

Nakamura

Gō

2005

Cell. Mol. Life Sci.

242

140

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“…The latter enzyme undergoes a pH-dependent dimerization, with the dimer predominating in a pH range of 5.0-8.0. Homodimeric laccases whose subunits account for two domain laccases have been purified from Pleurotus pulmonarius [18], Pleurotus eryngii [111], and from the mycorrhizal fungus Cantharellus cibarius [112]. These enzymes seem to need dimerization to exploit their function.…”

Section: Atypical Laccasesmentioning

confidence: 99%

Laccases: a never-ending story

Giardina¹,

Faraco²,

Pezzella³

et al. 2009

Cell. Mol. Life Sci.

866

638

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Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.

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“…Gel filtration on an FPLC-Superdex 75 column, which had been calibrated with molecular mass markers (GE Healthcare), was conducted to determine the molecular mass of the lectin. The N-terminal sequence of the lectin was determined by using a Hewlett-Packard HP G1000A Edman degradation unit and an HP 1000 HPLC System [24].…”

Section: Determination Of Molecular Mass and N-terminal Sequencementioning

confidence: 99%

Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis

Zhao

et al. 2011

J. Basic Microbiol.

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A thermostable novel lectin with a molecular weight of 30.4 kDa was isolated from dried fruiting bodies of Agaricus arvensis. It was a dimer made up of two 15.2 kDa subunits. The lectin was unadsorbed on DEAE-cellulose in 10 mM phosphate buffer (pH 7.5), subsequently adsorbed on CM-cellulose in 10 mM NaAc buffer (pH 4.6) and then on SP-Sepharose in 10 mM NaAc buffer (pH 4.6), and finally purified by fast protein liquid chromatography-gel filtration on Superdex 75. The hemagglutinating activity of the lectin was stable at temperatures up to 90 °C. The activity was preserved in concentrations of NaOH solution up to 50 mM, but was sensitive to HCl and declined to 12.5% in 12.5 mM HCl. The activity was unaffected by Ca(2+), Mn(2+), Zn(2+) and Mg(2+) ions, but was activated by Al(3+) and Fe(3+) ions. Among the carbohydrates tested, only inulin could inhibit the hemagglutinating activity of the lectin. It did not exhibit anti-HIV reverse transcriptase activity. Proliferation of HepG2 and MCF7 tumor cells was inhibited by the lectin with an IC(50) of 1.64 and 0.82 μM, respectively. The lectin was devoid of antifungal activity. The lectin has a remarkable thermostablity and a unique N-terminal amino acid sequence, TYAVLNFVYG. The present report is the first report on a lectin from wild mushroom Agaricus arvensis.

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A homodimeric laccase with unique characteristics from the yellow mushroom Cantharellus cibarius

Cited by 69 publications

References 33 publications

Function and molecular evolution of multicopper blue proteins

Function and molecular evolution of multicopper blue proteins

Laccases: a never-ending story

Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis

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