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Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles

Studies on the substrate selectivity of recombinant ferrous-iron- and 2-oxoglutarate-dependent proline hydroxylases (PHs) reveal that they can catalyse the production of dihydroxylated 5-, 6-, and 7-membered ring products, and can accept bicyclic substrates. Ring-substituted substrate analogues (suc...

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Detalles Bibliográficos
Autores principales: Smart, Tristan J., Hamed, Refaat B., Claridge, Timothy D.W., Schofield, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6958525/
https://www.ncbi.nlm.nih.gov/pubmed/31706681
http://dx.doi.org/10.1016/j.bioorg.2019.103386
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author Smart, Tristan J.
Hamed, Refaat B.
Claridge, Timothy D.W.
Schofield, Christopher J.
author_facet Smart, Tristan J.
Hamed, Refaat B.
Claridge, Timothy D.W.
Schofield, Christopher J.
author_sort Smart, Tristan J.
collection PubMed
description Studies on the substrate selectivity of recombinant ferrous-iron- and 2-oxoglutarate-dependent proline hydroxylases (PHs) reveal that they can catalyse the production of dihydroxylated 5-, 6-, and 7-membered ring products, and can accept bicyclic substrates. Ring-substituted substrate analogues (such hydroxylated and fluorinated prolines) are accepted in some cases. The results highlight the considerable, as yet largely untapped, potential for amino acid hydroxylases and other 2OG oxygenases in biocatalysis.
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spelling pubmed-69585252020-01-17 Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles Smart, Tristan J. Hamed, Refaat B. Claridge, Timothy D.W. Schofield, Christopher J. Bioorg Chem Article Studies on the substrate selectivity of recombinant ferrous-iron- and 2-oxoglutarate-dependent proline hydroxylases (PHs) reveal that they can catalyse the production of dihydroxylated 5-, 6-, and 7-membered ring products, and can accept bicyclic substrates. Ring-substituted substrate analogues (such hydroxylated and fluorinated prolines) are accepted in some cases. The results highlight the considerable, as yet largely untapped, potential for amino acid hydroxylases and other 2OG oxygenases in biocatalysis. Elsevier 2020-01 /pmc/articles/PMC6958525/ /pubmed/31706681 http://dx.doi.org/10.1016/j.bioorg.2019.103386 Text en © 2019 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Smart, Tristan J.
Hamed, Refaat B.
Claridge, Timothy D.W.
Schofield, Christopher J.
Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
title Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
title_full Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
title_fullStr Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
title_full_unstemmed Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
title_short Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
title_sort studies on the selectivity of proline hydroxylases reveal new substrates including bicycles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6958525/
https://www.ncbi.nlm.nih.gov/pubmed/31706681
http://dx.doi.org/10.1016/j.bioorg.2019.103386
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