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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
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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. |
format | Online Article Text |
id | pubmed-6958525 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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