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The UDP-Glycosyltransferase (UGT) Superfamily: New Members, New Functions, and Novel Paradigms

Open access
Meech, Robyn, Hu, Dong Gui, McKinnon, Ross A., Mubarokah, Siti Nurul, Haines, Alex Z., Nair, Pramod C., Rowland, Andrew, Mackenzie, Peter I.·2019·Physiological Reviews

Abstract

UDP-glycosyltransferases (UGTs) catalyze the covalent addition of sugars to a broad range of lipophilic molecules. This biotransformation plays a critical role in elimination of a broad range of exogenous chemicals and by-products of endogenous metabolism, and also controls the levels and distribution of many endogenous signaling molecules. In mammals, the superfamily comprises four families: UGT1, UGT2, UGT3, and UGT8. UGT1 and UGT2 enzymes have important roles in pharmacology and toxicology including contributing to interindividual differences in drug disposition as well as to cancer risk. These UGTs are highly expressed in organs of detoxification (e.g., liver, kidney, intestine) and can be induced by pathways that sense demand for detoxification and for modulation of endobiotic signaling molecules. The functions of the UGT3 and UGT8 family enzymes have only been characterized relatively recently; these enzymes show different UDP-sugar preferences to that of UGT1 and UGT2 enzymes, and to date, their contributions to drug metabolism appear to be relatively minor. This review summarizes and provides critical analysis of the current state of research into all four families of UGT enzymes. Key areas discussed include the roles of UGTs in drug metabolism, cancer risk, and regulation of signaling, as well as the transcriptional and posttranscriptional control of UGT expression and function. The latter part of this review provides an in-depth analysis of the known and predicted functions of UGT3 and UGT8 enzymes, focused on their likely roles in modulation of levels of endogenous signaling pathways.

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Metadata

Authors
Meech, R., Hu, D. G., McKinnon, R. A., Mubarokah, S. N., Haines, A. Z., Nair, P. C., Rowland, A., & Mackenzie, P. I.
Venue
Physiological Reviews
Published
2019-04-01
Volume
99
Issue
2
Pages
1153-1222
ISSN
  • 0031-9333 (ISSN-L)
  • 1522-1210
OpenAlex
W2914241247
Cited by
368
References
31
FWCI
8.35
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The UDP-Glycosyltransferase (UGT) Superfamily: New Members, New Functions, and Novel Paradigms. https://app.cochat.ai/papers/10.1152/physrev.00058.2017
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Meech, R., Hu, D. G., McKinnon, R. A., Mubarokah, S. N., Haines, A. Z., Nair, P. C., Rowland, A., & Mackenzie, P. I. (2019). The UDP-Glycosyltransferase (UGT) Superfamily: New Members, New Functions, and Novel Paradigms. Physiological Reviews. https://doi.org/10.1152/physrev.00058.2017

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