(19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode

The final step in the biosynthesis of l-carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, γ-butyrobetaine hydroxylase (BBOX). (1)H and (19)F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in subst...

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Autores principales: Leśniak, Robert K., Rydzik, Anna M., Kamps, Jos J. A. G., Kahn, Amjad, Claridge, Timothy D. W., Schofield, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927413/
https://www.ncbi.nlm.nih.gov/pubmed/31702759
http://dx.doi.org/10.1039/c9cc06466d
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author Leśniak, Robert K.
Rydzik, Anna M.
Kamps, Jos J. A. G.
Kahn, Amjad
Claridge, Timothy D. W.
Schofield, Christopher J.
author_facet Leśniak, Robert K.
Rydzik, Anna M.
Kamps, Jos J. A. G.
Kahn, Amjad
Claridge, Timothy D. W.
Schofield, Christopher J.
author_sort Leśniak, Robert K.
collection PubMed
description The final step in the biosynthesis of l-carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, γ-butyrobetaine hydroxylase (BBOX). (1)H and (19)F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding. The value of the (19)F NMR methods is demonstrated by their use in the design of new BBOX inhibitors.
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spelling pubmed-69274132020-01-30 (19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode Leśniak, Robert K. Rydzik, Anna M. Kamps, Jos J. A. G. Kahn, Amjad Claridge, Timothy D. W. Schofield, Christopher J. Chem Commun (Camb) Chemistry The final step in the biosynthesis of l-carnitine in humans is catalysed by the 2-oxoglutarate and ferrous iron dependent oxygenase, γ-butyrobetaine hydroxylase (BBOX). (1)H and (19)F NMR studies inform on the BBOX mechanism including by providing evidence for cooperativity between monomers in substrate/some inhibitor binding. The value of the (19)F NMR methods is demonstrated by their use in the design of new BBOX inhibitors. Royal Society of Chemistry 2019-12-21 2019-11-08 /pmc/articles/PMC6927413/ /pubmed/31702759 http://dx.doi.org/10.1039/c9cc06466d Text en This journal is © The Royal Society of Chemistry 2019 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Leśniak, Robert K.
Rydzik, Anna M.
Kamps, Jos J. A. G.
Kahn, Amjad
Claridge, Timothy D. W.
Schofield, Christopher J.
(19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
title (19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
title_full (19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
title_fullStr (19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
title_full_unstemmed (19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
title_short (19)F NMR studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
title_sort (19)f nmr studies on γ-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927413/
https://www.ncbi.nlm.nih.gov/pubmed/31702759
http://dx.doi.org/10.1039/c9cc06466d
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