Compounds > 6-hydroxydopa quinone
Page last updated: 2024-09-03

6-hydroxydopa quinone and tyrosine

6-hydroxydopa quinone has been researched along with tyrosine in 13 studies

Compound Research Comparison

Studies
(6-hydroxydopa quinone)		Trials
(6-hydroxydopa quinone)		Recent Studies (post-2010)
(6-hydroxydopa quinone)		Studies
(tyrosine)		Trials
(tyrosine)		Recent Studies (post-2010) (tyrosine)
14401444,2738468,225

Research

Studies (13)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's6 (46.15)18.2507
2000's5 (38.46)29.6817
2010's2 (15.38)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Brown, DE; Dooley, DM; Janes, SM; Klinman, JP; Mu, D; Smith, AJ1
Aizenman, E; Newcomer, TA; Rosenberg, PA1
Fukui, T; Matsuzaki, R; Ozaki, Y; Sato, H; Tanizawa, K1
Eklund, H; Fontecave, M1
Dooley, DM; Freeman, HC; Guss, JM; Matsunami, H; McIntire, WS; Ruggiero, CE; Tanizawa, K; Wilce, MC; Yamaguchi, H1
Dooley, DM1
Dove, JE; Klinman, JP; Schwartz, B1
Chen, Z; Klinman, JP; Li, R; Mathews, FS; Schwartz, B; Williams, NK1
Klinman, JP; Samuels, NM2
DuBois, JL; Klinman, JP1
Chen, ZW; Datta, S; Dubois, JL; Klinman, JP; Mathews, FS1
Cai, H; Fu, Z; Xu, F1

Reviews

2 review(s) available for 6-hydroxydopa quinone and tyrosine

ArticleYear
Copper amine oxidase: a novel use for a tyrosine.
    Structure (London, England : 1993), 1995, Nov-15, Volume: 3, Issue:11

    Topics: Amine Oxidase (Copper-Containing); Bacterial Proteins; Binding Sites; Catalysis; Dihydroxyphenylalanine; Escherichia coli; Models, Chemical; Oxidation-Reduction; Protein Conformation; Quaternary Ammonium Compounds; Tyrosine

1995
Structure and biogenesis of topaquinone and related cofactors.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 1999, Volume: 4, Issue:1

    Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Galactose Oxidase; Lysine; Mechanics; Models, Molecular; Oxidation-Reduction; Quinones; Tyrosine

1999

Other Studies

11 other study(ies) available for 6-hydroxydopa quinone and tyrosine

ArticleYear
Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases.
    The Journal of biological chemistry, 1992, Apr-25, Volume: 267, Issue:12

    Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Binding Sites; Cell Line; Chromatography, High Pressure Liquid; Codon; Dihydroxyphenylalanine; Electrophoresis, Polyacrylamide Gel; Molecular Sequence Data; Pichia; Protein Processing, Post-Translational; Sequence Homology, Nucleic Acid; Spectrum Analysis, Raman; Tyrosine

1992
TOPA quinone, a kainate-like agonist and excitotoxin is generated by a catecholaminergic cell line.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 1995, Volume: 15, Issue:4

    Topics: Adrenal Gland Neoplasms; Animals; Aromatic Amino Acid Decarboxylase Inhibitors; Catecholamines; Chromatography, High Pressure Liquid; Dihydroxyphenylalanine; Glutathione; Hydrazines; Kinetics; PC12 Cells; Pheochromocytoma; Rats; Tyrosine

1995
Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue.
    FEBS letters, 1994, Sep-12, Volume: 351, Issue:3

    Topics: Arthrobacter; Coenzymes; Copper; Dihydroxyphenylalanine; Escherichia coli; Monoamine Oxidase; Oxidation-Reduction; Recombinant Proteins; Spectrum Analysis; Tyrosine

1994
Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone.
    Biochemistry, 1997, Dec-23, Volume: 36, Issue:51

    Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Apoenzymes; Arthrobacter; Binding Sites; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Dimerization; Hydrogen Bonding; Metalloproteins; Molecular Sequence Data; Protein Conformation; Protein Processing, Post-Translational; Sequence Alignment; Substrate Specificity; Tyrosine

1997
Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast.
    Biochemistry, 2000, Apr-04, Volume: 39, Issue:13

    Topics: Amine Oxidase (Copper-Containing); Binding Sites; Coenzymes; Copper; Deuterium; Dihydroxyphenylalanine; Enzyme Precursors; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Oxygen; Oxygen Consumption; Pichia; Solvents; Temperature; Tyrosine; Viscosity

2000
Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.
    Biochemistry, 2000, Aug-15, Volume: 39, Issue:32

    Topics: Amine Oxidase (Copper-Containing); Catalytic Domain; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Models, Molecular; Oxidation-Reduction; Pichia; Protein Processing, Post-Translational; Recombinant Proteins; Tyrosine; Zinc

2000
2,4,5-Trihydroxyphenylalanine quinone biogenesis in the copper amine oxidase from Hansenula polymorpha with the alternate metal nickel.
    Biochemistry, 2005, Nov-01, Volume: 44, Issue:43

    Topics: Amine Oxidase (Copper-Containing); Binding Sites; Dihydroxyphenylalanine; Kinetics; Metals; Nickel; Oxygen; Pichia; Protein Processing, Post-Translational; Tyrosine

2005
Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha.
    Biochemistry, 2006, Mar-14, Volume: 45, Issue:10

    Topics: Amine Oxidase (Copper-Containing); Binding Sites; Catalysis; Coenzymes; Conserved Sequence; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Ethylamines; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Phenylhydrazines; Pichia; Tyrosine

2006
Investigation of Cu(I)-dependent 2,4,5-trihydroxyphenylalanine quinone biogenesis in Hansenula polymorpha amine oxidase.
    The Journal of biological chemistry, 2006, Jul-28, Volume: 281, Issue:30

    Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Kinetics; Models, Chemical; Pichia; Spectrophotometry; Superoxides; Tyrosine; Ultraviolet Rays

2006
Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
    Biochemistry, 2010, Aug-31, Volume: 49, Issue:34

    Topics: Amine Oxidase (Copper-Containing); Binding Sites; Copper; Dihydroxyphenylalanine; Mutation; Oxidation-Reduction; Oxygenases; Pichia; Tyrosine

2010
Cu(II)-mediated phenol oxygenation: chemical evidence implicates a unique role of the enzyme active site in promoting the chemically difficult tyrosine monooxygenation in TPQ cofactor biogenesis of copper amine oxidases.
    Bioorganic chemistry, 2015, Volume: 59

    Topics: Amine Oxidase (Copper-Containing); Catalytic Domain; Coenzymes; Copper; Dihydroxyphenylalanine; Oxidation-Reduction; Oxygen; Phenols; Tyrosine

2015