Human cytosolic sulfotransferase SULT1A1

Nadine Hempel, Niranjali Gamage, Jennifer L. Martin, Michael E. McManus

Research output: Contribution to journalShort survey

31 Citations (Scopus)

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 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.

Original languageEnglish (US)
Pages (from-to)685-689
Number of pages5
JournalInternational Journal of Biochemistry and Cell Biology
Volume39
Issue number4
DOIs
StatePublished - Mar 12 2007

Fingerprint

Sulfotransferases
Sulfonation
Enzymes
Biological Phenomena
Mutagenesis
DNA Adducts
Polycyclic Aromatic Hydrocarbons
Xenobiotics
Substrates
Substrate Specificity
Metabolism
Carcinogens
Catalyst activity
Estrogens
Crystal structure
human SULT1A1 protein
Neoplasms

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology

Cite this

Hempel, Nadine ; Gamage, Niranjali ; Martin, Jennifer L. ; McManus, Michael E. / Human cytosolic sulfotransferase SULT1A1. In: International Journal of Biochemistry and Cell Biology. 2007 ; Vol. 39, No. 4. pp. 685-689.
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Human cytosolic sulfotransferase SULT1A1. / Hempel, Nadine; Gamage, Niranjali; Martin, Jennifer L.; McManus, Michael E.

In: International Journal of Biochemistry and Cell Biology, Vol. 39, No. 4, 12.03.2007, p. 685-689.

Research output: Contribution to journalShort survey

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AU - Hempel, Nadine

AU - Gamage, Niranjali

AU - Martin, Jennifer L.

AU - McManus, Michael E.

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N2 - 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.

AB - 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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