Page last updated: 2024-08-17

methionine and laccase

methionine has been researched along with laccase in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19901 (14.29)18.7374
1990's0 (0.00)18.2507
2000's3 (42.86)29.6817
2010's1 (14.29)24.3611
2020's2 (28.57)2.80

Authors

AuthorsStudies
Co, MS; Hodgson, KO; Solomon, EI; Spira, DJ1
Antonyuk, S; Dodd, FE; Hall, JF; Hasnain, SS; Hough, MA; Kanbi, LD1
Koul, S; Lehnig, M; Müller, GH; Völkert, M; Waldmann, H1
Ivanic, J; Jensen, JH; Li, H; Webb, SP1
Dong, Y; Fan, Y; Gao, Z; Gong, Y; Liu, X; Tian, J; Wang, H; Wu, N; Yan, Y; Yue, Q; Zhang, Z; Zhao, J1
Avelar, M; Miranda-Blancas, R; Rodriguez-Arteaga, A; Rudiño-Piñera, E; Sinicropi, A1
Xie, Y; Xu, Z; Yang, S; Yu, H; Zhou, J1

Other Studies

7 other study(ies) available for methionine and laccase

ArticleYear
EXAFS investigation of the binuclear cupric site in met T2D Rhus laccase and its azide bound derivative.
    Biochemical and biophysical research communications, 1983, Apr-29, Volume: 112, Issue:2

    Topics: Azides; Binding Sites; Chemical Phenomena; Chemistry; Copper; Hemocyanins; Laccase; Methionine; Oxidoreductases; Plants, Toxic; Spectrum Analysis; Toxicodendron; X-Rays

1983
Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins.
    Journal of molecular biology, 2002, Jul-05, Volume: 320, Issue:2

    Topics: Amino Acid Sequence; Aspartic Acid; Azurin; Binding Sites; Ceruloplasmin; Copper; Crystallography, X-Ray; Hydrogen Bonding; Laccase; Leucine; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Mutation; Nitrite Reductases; Oxidation-Reduction; Oxidoreductases; Phylogeny; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine; Thiobacillus

2002
Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis.
    The Journal of organic chemistry, 2002, Oct-04, Volume: 67, Issue:20

    Topics: Agaricales; Amino Acids; Catalysis; Chemistry, Organic; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Hydrolysis; Laccase; Methionine; Molecular Structure; Monophenol Monooxygenase; Oxidation-Reduction; Oxidoreductases; Oxygen; Peptides; Phenylhydrazines; Temperature

2002
Determinants of the relative reduction potentials of type-1 copper sites in proteins.
    Journal of the American Chemical Society, 2004, Jun-30, Volume: 126, Issue:25

    Topics: Azurin; Binding Sites; Ceruloplasmin; Copper; Cysteine; Humans; Hydrogen Bonding; Laccase; Ligands; Methionine; Oxidation-Reduction; Plastocyanin; Proteins; Quantum Theory

2004
Crystal structures of multicopper oxidase CueO G304K mutant: structural basis of the increased laccase activity.
    Scientific reports, 2018, 09-24, Volume: 8, Issue:1

    Topics: Amino Acid Sequence; Binding Sites; Copper; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Laccase; Methionine; Models, Molecular; Mutation; Oxidoreductases; Protein Conformation; Protein Structure, Tertiary; Substrate Specificity

2018
The β-hairpin from the Thermus thermophilus HB27 laccase works as a pH-dependent switch to regulate laccase activity.
    Journal of structural biology, 2021, Volume: 213, Issue:2

    Topics: Amino Acid Motifs; Bacterial Proteins; Crystallography, X-Ray; Hydrazones; Hydrogen-Ion Concentration; Laccase; Methionine; Molecular Dynamics Simulation; Oxidation-Reduction; Oxidoreductases; Phylogeny; Protein Conformation; Temperature; Thermus thermophilus

2021
Modulating the adsorption orientation of methionine-rich laccase by tailoring the surface chemistry of single-walled carbon nanotubes.
    Colloids and surfaces. B, Biointerfaces, 2022, Volume: 217

    Topics: Adsorption; Electrodes; Laccase; Methionine; Nanotubes, Carbon

2022