Sulfotransferase 1A1

Definition:

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin. Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis. May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system.

References:

[1]. M H Kester, et al. Characterization of human iodothyronine sulfotransferases. J Clin Endocrinol Metab. 1999 Apr;84(4):1357-64. [Content Brief]

[2]. Ilana Berger, et al. The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. PLoS One. 2011;6(11):e26794. [Content Brief]

[3]. Brittany D Needham, et al. A gut-derived metabolite alters brain activity and anxiety behaviour in mice. Nature. 2022 Feb;602(7898):647-653. [Content Brief]

[4]. Uria Alcolombri, et al. Directed evolution of sulfotransferases and paraoxonases by ancestral libraries. J Mol Biol. 2011 Aug 26;411(4):837-53. [Content Brief]

[5]. H C Chou, et al. Metabolic activation of N-hydroxy arylamines and N-hydroxy heterocyclic amines by human sulfotransferase(s). Cancer Res. 1995 Feb 1;55(3):525-9. [Content Brief]

[6]. Niranjali U Gamage, et al. Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition. J Biol Chem. 2003 Feb 28;278(9):7655-62. [Content Brief]

[7]. Niranjali U Gamage, et al. The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates. J Biol Chem. 2005 Dec 16;280(50):41482-6. [Content Brief]

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