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

Nutrition

Journal of Nutritional Disorders & Therapy

Author(s): Riley PA

Abstract Share this page

Abstract A mathematical model of phase I melanogenesis is described based on the differential reactivity of tyrosinase according to the redox status of the active site copper atoms shown by Lerch and co-workers (see Lerch, 1981, Metal Ions in Biological Systems (Sigel, H., ed.) Vol. 13, pp. 143-186. New York: Marcel Dekker) in combination with the indirect formation of the catecholic intermediate substrate. In this model the unusual autoactivation kinetics of tyrosinase are explained by recruitment of enzyme from the met -form, in which the active-site copper atoms are in the oxidized (Cu(II)) state, by 2-electron donation from catechol oxidation. Using estimates of the values for the rate constants of the six reactions involved, the general characteristics of the model are shown to be consistent with the kinetic behaviour of tyrosinase in vitro. These include a lag period which is sensitive to catechol addition. This article was published in J Theor Biol and referenced in Journal of Nutritional Disorders & Therapy

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Relevant Topics

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords