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

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    Publication date
    2020-01
    Author
    Smart, T.J.
    Hamed, Refaat B.
    Claridge, T.D.W.
    Schofield, C.J.
    Keyword
    2-Oxoglutarate oxygenases
    Amino acid oxidation
    Biocatalysis
    L-proline
    Proline hydroxylase
    Rights
    (c) 2020 The Authors. This is an Open Access article distributed under the Creative Commons CC-BY license (https://creativecommons.org/licenses/by/4.0/)
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    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.
    URI
    http://hdl.handle.net/10454/17659
    Version
    Published version
    Citation
    Smart TJ, Hamed RB, Claridge TDW et al (2020) Studies on the selectivity of proline hydroxylases reveal new substrates including bicycles. Bioorganic Chemistry. 94: 103386.
    Link to publisher’s version
    https://doi.org/10.1016/j.bioorg.2019.103386
    Type
    Article
    Collections
    Life Sciences Publications

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