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

[1]  Robert J. Deeth,et al.  Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations , 2010, JBIC Journal of Biological Inorganic Chemistry.

[2]  J. Munoz-Munoz,et al.  Generation of hydrogen peroxide in the melanin biosynthesis pathway. , 2009, Biochimica et biophysica acta.

[3]  R. Varón,et al.  A review on spectrophotometric methods for measuring the monophenolase and diphenolase activities of tyrosinase. , 2007, Journal of agricultural and food chemistry.

[4]  Heinz Decker,et al.  The first crystal structure of tyrosinase: all questions answered? , 2006, Angewandte Chemie.

[5]  R. Varón,et al.  Calculating molar absorptivities for quinones: application to the measurement of tyrosinase activity. , 2006, Analytical biochemistry.

[6]  Y. Matoba,et al.  Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis* , 2006, Journal of Biological Chemistry.

[7]  F. García-Cánovas,et al.  Deuterium isotope effect on the oxidation of monophenols and o-diphenols by tyrosinase. , 2004, The Biochemical journal.

[8]  F. García-Cánovas,et al.  Solvent deuterium isotope effect on the oxidation of o-diphenols by tyrosinase. , 2003, Biochimica et biophysica acta.

[9]  R. Varón,et al.  Analysis and interpretation of the action mechanism of mushroom tyrosinase on monophenols and diphenols generating highly unstable o-quinones. , 2001, Biochimica et biophysica acta.

[10]  R. Varón,et al.  Stopped-Flow and Steady-State Study of the Diphenolase Activity of Mushroom Tyrosinase† , 2000 .

[11]  E. Solomon,et al.  Multicopper Oxidases and Oxygenases. , 1996, Chemical reviews.

[12]  Daniel L. Purich,et al.  Contemporary enzyme kinetics and mechanism , 1996 .

[13]  J N Rodríguez-López,et al.  Tyrosinase: a comprehensive review of its mechanism. , 1995, Biochimica et biophysica acta.

[14]  F. García-Cánovas,et al.  Tyrosinase: kinetic analysis of the transient phase and the steady state. , 1994, Biochimica et biophysica acta.

[15]  R. Varón,et al.  Calibration of a Clark-Type oxygen electrode by tyrosinase-catalyzed oxidation of 4-tert-butylcatechol. , 1992, Analytical biochemistry.

[16]  R. Varón,et al.  Analysis of a kinetic model for melanin biosynthesis pathway. , 1992, The Journal of biological chemistry.

[17]  F. García-Carmona,et al.  The role of pH in the melanin biosynthesis pathway. , 1982, The Journal of biological chemistry.

[18]  F. García-Carmona,et al.  Kinetic study of the pathway of melanizationn between l-dopa and dopachrome , 1982 .

[19]  E. Schaftingen,et al.  Control of liver 6-phosphofructokinase by fructose 2,6-bisphosphate and other effectors. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[20]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[21]  G. M. Walton,et al.  KINETICS OF REGULATORY ENZYMES. ESCHERICHIA COLI PHOSPHOFRUCTOKINASE. , 1965, The Journal of biological chemistry.

[22]  D. E. Atkinson,et al.  THE EFFECT OF ADENYLIC ACID ON YEAST NICOTINAMIDE ADENINE DINUCLEOTIDE ISOCITRATE DEHYDROGENASE, A POSSIBLE METABOLIC CONTROL MECHANISM. , 1963, The Journal of biological chemistry.

[23]  Wolfe Rg,et al.  Some molecular and kinetic properties of heart malic dehydrogenase. , 1956 .