Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi

Glazunova, Olga A.; Polyakov, K. M.; Moiseenko, Konstantin V.; Kurzeev, S. A.; Федорова, Т. В.

doi:10.1016/j.ijbiomac.2018.06.038

Cited by 23 publications

(30 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The basidiomycete S. murashkinskyi strain LE-BIN 1963 was obtained from the Collection of the Komarov Botanical Institute, Russian Academy of Sciences, St Petersburg, Russia. Cultivation of the strain was carried out as described in Glazunova et al (2018). In the first stage, the laccase was purified by ion-exchange chromatography on DEAE Cellulose (batch) and DEAE Toyopearl 650M (Tosoh, Japan) as described in Koroljova-Skorobogat'ko et al (1998).…”

Section: Culture Conditions and Enzyme Purificationmentioning

confidence: 99%

“…Refinement was performed with REFMAC5 (Murshudov et al, 2011) using the previously solved structure of S. murashkinskyi laccase (Glazunova et al, 2018; PDB entry 5e9n). In the final stages the temperature factors were refined using an anisotropic approach for copper ions, most of the atoms with full occupancy (relatively low temperature factors) and ligands in the TNC with an occupancy of greater than 0.4.…”

Section: X-ray Diffraction Data Collection and Structure Refinementmentioning

confidence: 99%

“…1 for the laccase from the basidiomycete fungus Steccherinum murashkinskyi. Its structure has recently been solved at high resolution from X-ray data (Glazunova et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism

Polyakov

Gavryushov

Федорова

et al. 2019

Acta Crystallogr D Struct Biol

Self Cite

View full text Add to dashboard Cite

Laccases are enzymes that catalyze the oxidation of a wide range of organic and inorganic substrates accompanied by the reduction of molecular oxygen to water. Here, a subatomic resolution X‐ray crystallographic study of the mechanism of inhibition of the laccase from the basidiomycete fungus Steccherinum murashkinskyi by chloride and fluoride ions is presented. Three series of X‐ray diffraction data sets were collected with increasing doses of absorbed X‐ray radiation from a native S. murashkinskyi laccase crystal and from crystals of complexes of the laccase with chloride and fluoride ions. The data for the native laccase crystal confirmed the previously deduced enzymatic mechanism of molecular oxygen reduction. The structures of the complexes allowed the localization of chloride and fluoride ions in the channel near the T2 copper ion. These ions replace the oxygen ligand of the T2 copper ion in this channel and can play the role of this ligand in the enzymatic reaction. As follows from analysis of the structures from the increasing dose series, the inhibition of laccases by chloride and fluoride anions can be explained by the fact that the binding of these negatively charged ions at the position of the oxygen ligand of the T2 copper ion impedes the reduction of the T2 copper ion.

show abstract

Section: Culture Conditions and Enzyme Purificationmentioning

confidence: 99%

Section: X-ray Diffraction Data Collection and Structure Refinementmentioning

confidence: 99%

See 1 more Smart Citation

The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism

Polyakov

Gavryushov

Федорова

et al. 2019

Acta Crystallogr D Struct Biol

Self Cite

View full text Add to dashboard Cite

show abstract

“…The lower energy configurations and high binding model of LAC3 with the aflatoxin was considered as the most likely optimized LAC3 and this can be seen from Figure 3. In our models, the oxygen atom of the methoxy group of AFB 1 , regarded as hydrogen bond acceptor, forms one hydrogen bond with the side chain of His481, which is coordinated to the nearby copper ion (i.e., T1 Cu II ) (Glazunova, Polyakov, Moiseenko, Kurzeev, & Fedorova, 2018), whereas the oxygen atom of the terminal furan ring, regarded as hydrogen bond acceptor, forms one hydrogen bond with the side chain of Asn288. Similarly, a carbon atom of the benzene ring in AFB 2 , regarded as hydrogen bond acceptor, forms one hydrogen bond with the sidechain of His481.…”

Section: Resultsmentioning

confidence: 99%

Molecular docking studies and in vitro degradation of four aflatoxins (AFB₁, AFB₂, AFG₁, and AFG₂) by a recombinant laccase from Saccharomyces cerevisiae

Liu

Mao

et al. 2020

Journal of Food Science

View full text Add to dashboard Cite

Here, molecular docking simulation was used to predict and compare interactions between a recombinant Trametes sp. C30 laccase from Saccharomyces cerevisiae and four aflatoxins (AFB 1 , AFB 2 , AFG 1 , and AFG 2 ) as well as their degradation at a molecular level. The computational result of docking simulation indicates that each of the aflatoxins tested can interact with laccase with a binding ability of AFB 1 >AFG 2 >AFG 1 >AFB 2 . Simultaneously, it also demonstrated that aflatoxin B 1 , B 2 , G 1 , G 2 may interact near the T1 copper center of the enzyme through H-bonds and hydrophobic interactions with amino acid residues His481 and Asn288; His481; Asn288, and Asp230; His481 and Asn288. Biological degradation test was performed in vitro in the presence of a recombinant laccase. Degradation increased as incubation time increased from 12 to 60 hr and the maximum degradation obtained for AFB 1 , AFB 2 , AFG 1 , and AFG 2 was 90.33%, 74.23%, 85.24%, and 87.58%, respectively. Maximum degradation of aflatoxins was determined with a total activity 3 U laccase at 30°C in 0.1 M phosphate buffer, pH 5.7 after 48-hr incubation. The experimental results are consistent with that of docking calculation on the biological degradation test of four aflatoxins by laccase.Practical Application: In this study, the degradation efficiencies of laccase for B and G series of aflatoxins were determined by computer simulation and verified by performing in vitro experiments. It can provide reference for rapid screening of aflatoxin degradation-related enzymes.

show abstract

“…Despite the overall moderate sequence identity (~32%) and similarity (~50%) to available template structures, we were able to generate a model of Af_AO1. The five models built on two laccases from Steccherinum murashkinskyi (5E9N [38]…”

Section: Modeling Of Af_ao1mentioning

confidence: 99%

A Fungal Ascorbate Oxidase with Unexpected Laccase Activity

Braunschmid

Fuerst

Perz

et al. 2020

IJMS

View full text Add to dashboard Cite

Ascorbate oxidases are an enzyme group that has not been explored to a large extent. So far, mainly ascorbate oxidases from plants and only a few from fungi have been described. Although ascorbate oxidases belong to the well-studied enzyme family of multi-copper oxidases, their function is still unclear. In this study, Af_AO1, an enzyme from the fungus Aspergillus flavus, was characterized. Sequence analyses and copper content determination demonstrated Af_AO1 to belong to the multi-copper oxidase family. Biochemical characterization and 3D-modeling revealed a similarity to ascorbate oxidases, but also to laccases. Af_AO1 had a 10-fold higher affinity to ascorbic acid (KM = 0.16 ± 0.03 mM) than to ABTS (KM = 1.89 ± 0.12 mM). Furthermore, the best fitting 3D-model was based on the ascorbate oxidase from Cucurbita pepo var. melopepo. The laccase-like activity of Af_AO1 on ABTS (Vmax = 11.56 ± 0.15 µM/min/mg) was, however, not negligible. On the other hand, other typical laccase substrates, such as syringaldezine and guaiacol, were not oxidized by Af_AO1. According to the biochemical and structural characterization, Af_AO1 was classified as ascorbate oxidase with unusual, laccase-like activity.

show abstract

Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi

Cited by 23 publications

References 60 publications

The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism

The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism

Molecular docking studies and in vitro degradation of four aflatoxins (AFB₁, AFB₂, AFG₁, and AFG₂) by a recombinant laccase from Saccharomyces cerevisiae

A Fungal Ascorbate Oxidase with Unexpected Laccase Activity

Contact Info

Product

Resources

About

Structure-function study of two new middle-redox potential laccases from basidiomycetes Antrodiella faginea and Steccherinum murashkinskyi

Cited by 23 publications

References 60 publications

The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism

The subatomic resolution study of laccase inhibition by chloride and fluoride anions using single-crystal serial crystallography: insights into the enzymatic reaction mechanism

Molecular docking studies and in vitro degradation of four aflatoxins (AFB1, AFB2, AFG1, and AFG2) by a recombinant laccase from Saccharomyces cerevisiae

A Fungal Ascorbate Oxidase with Unexpected Laccase Activity

Contact Info

Product

Resources

About

Molecular docking studies and in vitro degradation of four aflatoxins (AFB₁, AFB₂, AFG₁, and AFG₂) by a recombinant laccase from Saccharomyces cerevisiae