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  • Human cytosolic sulfotransferase SULT1A1

    Author(s)
    Hempel, Nadine
    Gamage, Niranjali
    Martin, Jennifer L
    McManus, Michael E
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    2007
    Metadata
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    Abstract
    Sulfonation is an important conjugation reaction required for a range of biological processes including phase II metabolism, whereby sulfo-conjugation renders a compound more hydrophilic to aid its excretion. The major enzyme responsible for xenobiotic sulfonation is the widely expressed cytosolic sulfotransferase SULT1A1. The SULT1A1 crystal structure has provided insights into this enzyme's substrate specificity and catalytic function, including its role in the sulfonation of endogenous substrates such as oestrogens. Contrary to its metabolic role, SULT1A1 can also bioactivate compounds; it is known to sulfonate pro-carcinogens ...
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    Sulfonation is an important conjugation reaction required for a range of biological processes including phase II metabolism, whereby sulfo-conjugation renders a compound more hydrophilic to aid its excretion. The major enzyme responsible for xenobiotic sulfonation is the widely expressed cytosolic sulfotransferase SULT1A1. The SULT1A1 crystal structure has provided insights into this enzyme's substrate specificity and catalytic function, including its role in the sulfonation of endogenous substrates such as oestrogens. Contrary to its metabolic role, SULT1A1 can also bioactivate compounds; it is known to sulfonate pro-carcinogens such as hydroxymethyl polycyclic aromatic hydrocarbons leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis. Given the role of SULT1A1 in these diverse functions and the discovery of allelic variants with differing catalytic activities, this enzyme has been the focus of numerous polymorphic studies investigating the link between inter-individual SULT1A1 variance and the etiology of a variety of cancers.
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    Journal Title
    International Journal of Biochemistry & Cell Biology
    Volume
    39
    Issue
    4
    DOI
    https://doi.org/10.1016/j.biocel.2006.10.002
    Subject
    Biochemistry and cell biology
    Biochemistry and cell biology not elsewhere classified
    Medical biochemistry and metabolomics
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/347438
    Collection
    • Journal articles

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