Skin: Pigmentation

Recent papers on Tyrosinases or Polyphenol oxidases  (EC 1.14.18.1) published in scientific journals (from 1995). Tyrosinase is the enzyme starting the melanin biosynthesis pathway in humans, as well as the main regulatory enzyme of the melanogenesis that originates skin pigmentation, from healthy melanocytes and  tumoral melanocytes of melanoma, a very invasive skin cancer.

Tyrosinase: Regulation by Inhibition

Molecular docking studies of ortho-substituted phenols to tyrosinase helps discern if a molecule can be an enzyme substrate.

Int. J. Mol. Sci., 25(6891), 1-14, 2024. https://dx.doi.org/10.3390/ijms25136891

- Garcia-Jimenez, A., Teruel-Puche, J. A., Ortiz-Ruiz, C. V., Berna, J., Tudela, J., Garcia-Canovas, F.

Study of the inhibition of 3-/4-aminoacetophenones on tyrosinase.

Reaction Kinetics Mechanisms and Catalysis, 120(1), 1-13, 2017. https://dx.doi.org/10.1007/s11144-016-1106-6

Action of 2,2',4,4'-tetrahydroxybenzophenone in the biosynthesis pathway of melanin.

International Journal of Biological Macromolecules, 98, 622-629, 2017. https://dx.doi.org/10.1016/j.ijbiomac.2017.02.032

Further insight into the pH effect on the catalysis of mushroom tyrosinase.

J. Mol. Catal. B: Enzymatic, 125, 6-15, 2016. https://dx.doi.org/10.1016/j.molcatb.2015.12.008

Kinetic characterization of substrate-analogous inhibitors of tyrosinase.

IUBMB Life 67, 757-767, 2015. https://dx.doi.org/10.1002/iub.1432  

Discrimination between alternative substrates and inhibitors of tyrosinase.

Journal of Agricultural and Food Chemistry, 63, 2162-2171, 2015. https://dx.doi.org/10.1021/jf5051816  

Tyrosinase: Regulation by Inactivation

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

Biochimica et Biophysica Acta - Proteins and Proteomics, 1824, 647-655 (2012).

Tyrosinase inactivation in its action on tyrosine.

Acta Biochimica Polonica, 58(4):477-8, 2011.

Suicide inactivation of tyrosinase in its action on tetrahydropterines.

Journal of Enzyme Inhibition and Medicinal Chemistry, 26, 728-733, 2011.

Tetrahydrofolic Acid Is a Potent Suicide Substrate of Mushroom Tyrosinase.

Journal of Agricultural and Food Chemistry, 59, 1383-1391, 2011.

Suicide inactivation of the diphenolase and monophenolase activities of tyrosinase.

IUBMB Life, 62, 539-547, 2010.

Tyrosinase inactivation in its action on dopa.

Biochimica et Biophysica Acta-Proteins and Proteomics, 1804, 1467-1475, 2010.

Stereospecific inactivation of tyrosinase by L-and D-ascorbic acid.

Biochimica et Biophysica Acta - Proteins and Proteomics, 1794, 244-253, 2009.

Phenolic substrates and suicide inactivation of tyrosinase: kinetics and mechanism.

Biochemical Journal, 416, 431-440, 2008.


Tyrosinase: Regulation by Reaction Mechanism

Kinetic cooperativity of tyrosinase. A general mechanism.

Acta Biochimica Polonica, 58, 303-311, 2011. Polonia.

Generation of hydrogen peroxide in the melanin biosynthesis pathway.

Biochimica et Biophysica Acta - Proteins and Proteomics, 1794, 1017-1029, 2009. Holanda.

An approximate analytical solution to the lag period of monophenolase activity.

Int. J. Biochem. Cell Biology, 39, 238-252, 2007.

     A further step in the kinetic characterisation of the tyrosinase enzymatic system.

     Journal of Mathematical Chemistry, 44, 393-406, 2007.

Kinetic study of monophenol and o-diphenol binding to oxytyrosinase.

Journal of Molecular Catalysis B: Enzymatic, 35, 185-192, 2005.

Reaction mechanism to explain the high kinetic autoactivation of tyrosinase.

J. Mol. Catal.-B: Enzymatic, 32, 35-42, 2005.

Mushroom tyrosinase: catalase activity, inhibition and suicide inactivation.

J. Agric. Food Chem. 53, 3702-3709, 2005.

Tyrosinase kinetics: discrimination between two models to explain the oxidation mechanism of monophenol and diphenol substrates.

Int. J. Biochem. Cell Biol. 36, 235-246, 2004.

Solvent deuterium isotope effect on the oxidation of o-diphenols by tyrosinase.

Biochimica et Biophysica Acta, 1650, 128-135, 2003.

Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and diphenols.

Biochimica et Biophysica Acta,1597, 140-148, 2002.

Analysis and interpretation of the reaction mechanism of mushroom tyrosinase on monophenols and diphenols generating highly unstable o-quinones.

Biochim. Biophys. Acta, 1548, 1-22, 2001.

Tyrosinase action on monophenols: enzymatic release of o-diphenol.

Biochim. Biophys. Acta, 1549, 1-19, 2001.

Analysis and interpretation of the action mechanism of mushroom tyrosinase on monophenols and diphenols generating highly unstable o-quinones

Biochimica et Biophysica Acta 1548, 1-22, 2001.

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

Biochimica et Biophysica Acta 1548, 238-256, 2001.

Stopped-flow and steady-state study of the diphenolase activity of mushroom tyrosinase.

Biochemistry 39, 10497-10506, 2000.

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

European Journal of Biochemistry 267, 5865-5878, 2000.

Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase.

European Journal of Biochemistry 267, 1270-1279, 2000.

Monophenolase and diphenolase reaction mechanism of apple and pear polyphenol oxidases.

J. Agric. Food Chem. 46, 2968-2975, 1998.

Oxymetric and spectrophotometric study of the ascorbate oxidase activity shown by frog epidermis tyrosinase.

The International Journal of Biochemistry & Cell Biology, 28 (8), 917-923, 1996.

Tyrosinase: A comprehensive review of its mechanism.

Biochimica et Biophysica Acta 1247, 1-11, 1995.

 

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