Literature DB >> 3101741

A kinetic study of the melanization pathway between L-tyrosine and dopachrome.

J Cabanes, F García-Cánovas, J A Lozano, F García-Carmona.   

Abstract

In the pathway of melanin biosynthesis originating from L-tyrosine, the dopachrome accumulation at physiological pH is produced with a pronounced lag period, during which the level of L-dopa increases, following a sigmoidal kinetics to reach a steady-state. A kinetic model has been proposed for the overall pathway of melanization from L-tyrosine to dopachrome; it explains the lag period present during the dopachrome accumulation as well as the influence of L-tyrosine and tyrosinase over this lag period. Use of this model is also valid to explain the kinetics of L-dopa accumulation in the reaction medium, as has been tested by simulation.

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Year:  1987        PMID: 3101741     DOI: 10.1016/0304-4165(87)90003-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  22 in total

1.  The effect of substrate partitioning on the kinetics of enzymes acting in reverse micelles.

Authors:  R Bru; A Sánchez-Ferrer; F García-Carmona
Journal:  Biochem J       Date:  1990-06-15       Impact factor: 3.857

2.  Characterization of the monophenolase activity of tyrosinase on betaxanthins: the tyramine-betaxanthin/dopamine-betaxanthin pair.

Authors:  Fernando Gandía-Herrero; Josefa Escribano; Francisco García-Carmona
Journal:  Planta       Date:  2005-06-21       Impact factor: 4.116

3.  A kinetic study of irreversible enzyme inhibition by an inhibitor that is rendered unstable by enzymic catalysis. The inhibition of polyphenol oxidase by L-cysteine.

Authors:  E Valero; R Varón; F García-Carmona
Journal:  Biochem J       Date:  1991-08-01       Impact factor: 3.857

4.  The action of glycosylases on dopachrome (2-carboxy-2,3-dihydroindole-5,6-quinone) tautomerase.

Authors:  P Aroca; J H Martinez-Liarte; F Solano; J C García-Borrón; J A Lozano
Journal:  Biochem J       Date:  1992-05-15       Impact factor: 3.857

5.  First laccase in green algae: purification and characterization of an extracellular phenol oxidase from Tetracystis aeria.

Authors:  Benjamin Otto; Dietmar Schlosser
Journal:  Planta       Date:  2014-08-13       Impact factor: 4.116

6.  Discrimination between two kinetic mechanisms for the monophenolase activity of tyrosinase.

Authors:  J R Ros-Martínez; J N Rodríguez-López; R V Castellanos; F García-Cánovas
Journal:  Biochem J       Date:  1993-09-01       Impact factor: 3.857

7.  Betaxanthins as substrates for tyrosinase. An approach to the role of tyrosinase in the biosynthetic pathway of betalains.

Authors:  Fernando Gandía-Herrero; Josefa Escribano; Francisco García-Carmona
Journal:  Plant Physiol       Date:  2005-04-01       Impact factor: 8.340

8.  Unmasking the Effects of L-DOPA on Rapid Dopamine Signaling with an Improved Approach for Nafion Coating Carbon-Fiber Microelectrodes.

Authors:  Lingjiao Qi; Elina Thomas; Stephanie H White; Samantha K Smith; Christie A Lee; Leslie R Wilson; Leslie A Sombers
Journal:  Anal Chem       Date:  2016-08-03       Impact factor: 6.986

9.  Effect of L-ascorbic acid on the monophenolase activity of tyrosinase.

Authors:  J R Ros; J N Rodríguez-López; F García-Cánovas
Journal:  Biochem J       Date:  1993-10-01       Impact factor: 3.857

10.  Oxygen Michaelis constants for tyrosinase.

Authors:  J N Rodríguez-López; J R Ros; R Varón; F García-Cánovas
Journal:  Biochem J       Date:  1993-08-01       Impact factor: 3.857

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