Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase

The kinetic (KIE) and solvent (SIE) isotope effect methods were used to investigate the mechanism of enzymatic hydroxylation of halogenated derivatives of l-tyrosine to l-DOPA catalyzed by the enzyme tyrosinase (EC 1.14.18.1). The values of deuterium KIE and SIE were obtained using the non-competiti...

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Autores principales: Pająk, Małgorzata, Kańska, Marianna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5707235/
https://www.ncbi.nlm.nih.gov/pubmed/29213160
http://dx.doi.org/10.1007/s10967-017-5526-1
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author Pająk, Małgorzata
Kańska, Marianna
author_facet Pająk, Małgorzata
Kańska, Marianna
author_sort Pająk, Małgorzata
collection PubMed
description The kinetic (KIE) and solvent (SIE) isotope effect methods were used to investigate the mechanism of enzymatic hydroxylation of halogenated derivatives of l-tyrosine to l-DOPA catalyzed by the enzyme tyrosinase (EC 1.14.18.1). The values of deuterium KIE and SIE were obtained using the non-competitive method with spectrophotometric measurements. The Lineweaver–Burk plots were used for determination of the inhibition mode of 3′-iodo-l-tyrosine. Based upon kinetic effects values the mechanism of action of enzyme tyrosinase was proposed.
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spelling pubmed-57072352017-12-04 Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase Pająk, Małgorzata Kańska, Marianna J Radioanal Nucl Chem Article The kinetic (KIE) and solvent (SIE) isotope effect methods were used to investigate the mechanism of enzymatic hydroxylation of halogenated derivatives of l-tyrosine to l-DOPA catalyzed by the enzyme tyrosinase (EC 1.14.18.1). The values of deuterium KIE and SIE were obtained using the non-competitive method with spectrophotometric measurements. The Lineweaver–Burk plots were used for determination of the inhibition mode of 3′-iodo-l-tyrosine. Based upon kinetic effects values the mechanism of action of enzyme tyrosinase was proposed. Springer Netherlands 2017-10-23 2017 /pmc/articles/PMC5707235/ /pubmed/29213160 http://dx.doi.org/10.1007/s10967-017-5526-1 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Pająk, Małgorzata
Kańska, Marianna
Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
title Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
title_full Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
title_fullStr Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
title_full_unstemmed Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
title_short Isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
title_sort isotope effects in mechanistic studies of l-tyrosine halogen derivatives hydroxylation catalyzed by tyrosinase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5707235/
https://www.ncbi.nlm.nih.gov/pubmed/29213160
http://dx.doi.org/10.1007/s10967-017-5526-1
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AT kanskamarianna isotopeeffectsinmechanisticstudiesofltyrosinehalogenderivativeshydroxylationcatalyzedbytyrosinase

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