New features of the steady-state rate related with the initial concentration of substrate in the diphenolase and monophenolase activities of tyrosinase

Biochimica Et Biophysica Acta-protein Structure and Molecular Enzymology, 2001

Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase

European Journal of Biochemistry, 2000

Tyrosinase action on monophenols: evidence for direct enzymatic release of o-diphenol

Biochimica Et Biophysica Acta-protein Structure and Molecular Enzymology, 2001

Kinetic cooperativity of tyrosinase. A general mechanism

Acta Biochimica Polonica, 2011

Influencing the monophenolase/diphenolase activity ratio in tyrosinase

Margarita Kanteev

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013

Indirect inactivation of tyrosinase in its action on 4- tert -butylphenol

Jose Ramon Acosta Motos

Journal of Enzyme Inhibition and Medicinal Chemistry, 2013

Unification for the Expression of the Monophenolase and Diphenolase Activities of Tyrosinase

Iubmb Life, 2002

Tyrosinase kinetics: a semi-quantitative model of the mechanism of oxidation of monohydric and dihydric phenolic substrates

Patrick A. Riley

Journal of theoretical biology, 2000

Phenolic substrates and suicide inactivation of tyrosinase: kinetics and mechanism

Jose Tudela

Biochemical Journal, 2008

Michaelis constants of mushroom tyrosinase with respect to oxygen in the presence of monophenols and diphenols

International Journal of Biochemistry & Cell Biology, 2002

Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase

Peter Garratt, Patrick A. Riley

Journal of Biological …, 1997

Oxidation by mushroom tyrosinase of monophenols generating slightly unstable o-quinones

European Journal of Biochemistry, 2000

Considerations about the Continuous Assay Methods, Spectrophotometric and Spectrofluorometric, of the Monophenolase Activity of Tyrosinase

Jose Munoz

Biomolecules

Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone

IUBMB Life, 2014

Spectrophotometric determination of monophenolase activity of tyrosinase isozymes

James O Alben

Archives of Biochemistry and Biophysics, 1971

Kinetic characterisation of o-aminophenols and aromatic o-diamines as suicide substrates of tyrosinase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2012

Tyrosinase kinetics: failure of the auto-activation mechanism of monohydric phenol oxidation by rapid formation of a quinomethane intermediate

Patrick Riley

The Biochemical journal, 1998

Tyrosinase: The four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation

Patrick Riley

Bioorganic & Medicinal Chemistry, 2014

Direct spectrophotometric assay of monooxygenase and oxidase activities of mushroom tyrosinase in the presence of synthetic and natural substrates

Kamahldin Haghbeen

Analytical Biochemistry, 2003

SURVEYING ALLOSTERIC COOPERATIVITY AND COOPERATIVE INHIBITION IN MUSHROOM TYROSINASE

Mehdi Zareian Jahromi

Journal of Food Biochemistry, 2010

Mechanistic studies of the tyrosinase-catalyzed oxidative cyclocondensation of 2-aminophenol to 2-aminophenoxazin-3-one

Neil McIntyre

Archives of biochemistry and biophysics, 2015

Studies of the competing rates of catechol oxidation and suicide inactivation of tyrosinase

Patrick A. Riley

Arkivoc, 2010

Enzyme Kinetics of Crude Tyrosinase Extract

Lea Claire Te Roa

Kinetic Study of the Oxidation of γ- l -Glutaminyl-4-hydroxybenzene Catalyzed by Mushroom ( Agaricus bisporus ) Tyrosinase

Harry Wichers

Journal of Agricultural and Food Chemistry, 1999

Theoretical study of phenol and 2-aminophenol docking at a model of the tyrosinase active site

Jacques Maddaluno

New Journal of Chemistry, 2003

Hydroxylation of p-substituted phenols by tyrosinase: Further insight into the mechanism of tyrosinase activity

Biochemical and Biophysical Research Communications, 2012

The Relationship between the IC50 Values and the Apparent Inhibition Constant in the Study of Inhibitors of Tyrosinase Diphenolase Activity Helps Confirm the Mechanism of Inhibition

Molecules