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Enzyme Nomenclature
Information on EC 2.4.1.17 - glucuronosyltransferase
for references in articles please use BRENDA:EC2.4.1.17
Word Map on EC 2.4.1.17
- 2.4.1.17
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glucuronidation
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pharmacokinetics
- hyperbilirubinemia
- hepatocytes
- irinotecan
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drug-metabolizing
- phenobarbital
- gilbert
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biotransformation
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sulfotransferase
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carcinogen
- testosterone
- cyp3a4
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udp-glucuronic
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pharmacogenetic
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unconjugated
- cyp2c9
- neutropenia
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disposition
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extrahepatic
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benzoapyrene
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pregnane
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interindividual
- jaundice
- acetaminophen
- 3-methylcholanthrene
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o-deethylase
- androsterone
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drug-drug
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mycophenolic
- sult1a1
- 7-ethoxyresorufin
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herb-drug
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clint
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ethoxycoumarin
- raltegravir
- diagnostics
- atazanavir
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sults
- ethylmorphine
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endobiotics
- beta-naphthoflavone
- mofetil
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p-nitroanisole
- lamotrigine
- drug development
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androstane
- pharmacology
- propofol
- aminopyrine
- medicine
- codeine
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concentration-time
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cdna-expressed
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.4.1.17
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RECOMMENDED NAME
GeneOntology No.
glucuronosyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
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UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
sequential bireactant mechanism
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UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
aspartic acid residues, especially Asp150 and Asp488, and histidine residues mediate the acid-base reaction mechanism and the substrate specificity of the human subfamily of UDP-D-glucuronosyltransferases 1A catalyzing the nucleophilic attack of phenolic xenobiotics on UDP-D-glucuronic acid, leading to the formation of water-soluble glucuronides, overview; aspartic acid residues, especially Asp150 and Asp488, and histidine residues mediate the acid-base reaction mechanism and the substrate specificity of the human subfamily of UDP-D-glucuronosyltransferases 1A catalyzing the nucleophilic attack of phenolic xenobiotics on UDP-D-glucuronic acid, leading to the formation of water-soluble glucuronides, overview; aspartic acid residues, especially Asp150 and Asp488, and histidine residues mediate the acid-base reaction mechanism and the substrate specificity of the human subfamily of UDP-D-glucuronosyltransferases 1A catalyzing the nucleophilic attack of phenolic xenobiotics on UDP-D-glucuronic acid, leading to the formation of water-soluble glucuronides, overview; aspartic acid residues, especially Asp150 and Asp488, and histidine residues mediate the acid-base reaction mechanism and the substrate specificity of the human subfamily of UDP-D-glucuronosyltransferases 1A catalyzing the nucleophilic attack of phenolic xenobiotics on UDP-D-glucuronic acid, leading to the formation of water-soluble glucuronides, overview
UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
compulsory ordered bi bi mechanism
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UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
reaction mechanism, structure-activity relationship, docking of UDP-glucuronic acid to a model of isozyme UGT1A1
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UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
sequential bireactant mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronate beta-D-glucuronosyltransferase (acceptor-unspecific)
This entry denotes a family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines and fatty acids. Some of the activities catalysed were previously listed separately as EC 2.4.1.42, EC 2.4.1.59, EC 2.4.1.61, EC 2.4.1.76, EC 2.4.1.77, EC 2.4.1.84, EC 2.4.1.107 and EC 2.4.1.108. A temporary nomenclature for the various forms, whose delineation is in a state of flux, is suggested in Ref. 1.
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CAS REGISTRY NUMBER
COMMENTARY
37205-52-0
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37277-52-4
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37277-66-0
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61969-98-0
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62213-43-8
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62213-47-2
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9030-08-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Wistar strain
488695, 488697, 488698, 488701, 488703, 488706, 488707, 488711, 488712, 488715, 488717, 488719, 488720, 488721, 488723, 488724, 488730, 488734, 488735, 488736, 488737, 488739, 488740, 488746, 488750, 488752, 488762, 488792
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488696, 488707, 488709, 488720, 488743, 488761, 488762, 488763, 488772, 488778, 488780, 488783, 488785, 488786, 488787, 488788, 488789, 488792, 488795, 488799, 488801, 657879, 660431, 675039, 690857, 692032, 692044, 692786, 693111, 693817, 694249, 695269, 702016, 703017, 703403, 703404, 703407, 703410, 706097, 718805, 719346, 719347, 719348, 719349, 719350, 719352, 719760, 720115, 720303, 720334, 720509, 720625, 721114, 735944, 736006, 736015, 736672
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SwissProt
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SwissProt
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SwissProt
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SwissProt
isozyme UGT1A10; isozyme UGT1A10
SwissProt
isozyme UGT1A1; isozyme UGT1A1
SwissProt
isozyme UGT1A3; isozyme UGT1A3
SwissProt
isozyme UGT1A4; isozyme UGT1A4
SwissProt
isozyme UGT1A7; isozyme UGT1A7
SwissProt
isozyme UGT1A9; isozyme UGT1A9
SwissProt
isozyme UGT2B15; isozyme UGT2B15
SwissProt
isozyme UGT2B7; isozyme UGT2B7
SwissProt
isozymes UGT1A1, UGT1A7, UGT1A9, naturally occuring UGT1A9 mutant D256N, the latter from a japanese cancer patient
SwissProt
isozymes UGT1A9 and UGT2B7, renal transplant patients under mycopenolate mofetil therapy
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488696, 488704, 488732, 488733, 488744, 488748, 488749, 488756, 488758, 488760, 488764, 488779, 488780, 488784, 488787, 488790, 488793, 488794, 488798, 488799, 673287, 691045, 721077
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bilirubin UDP-glucuronosyltransferase not in Gunn strain; distribution in Wistar and Gunn strain; Gunn strain; Wistar strain
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bilirubin UDP-glucuronosyltransferase not in Gunn strain; Wistar strain
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Wistar strain
488695, 488697, 488698, 488701, 488706, 488712, 488715, 488719, 488720, 488721, 488723, 488724, 488730, 488734, 488735, 488737, 488739, 488740, 488750, 488752, 488762
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bilirubin UDP-glucuronosyltransferase not in Gunn strain; distribution in Wistar and Gunn strain; Gunn strain
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bilirubin UDP-glucuronosyltransferase not in Gunn strain; Gunn strain
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic; UGT enzymes are genetically polymorphic
evolution
feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution
evolution
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UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview
evolution
UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview; UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview; UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview; UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview; UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview
evolution
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UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview
evolution
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UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview
evolution
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UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview
evolution
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UGTs have been divided into two families: UGT1 and UGT2, based on similarities between their amino acid sequences and gene organization. Hepatic UGTactivity in the microminipig compared to those in humans and other experimental animals. Estradiol-3-glucuronidation activity is higher in the microminipig than in humans and other animals, serotonin glucuronide formation activity is 20-55fold higher in mouse and rat liver microsomes than in microsomes from the other animals. Glucuronidation activities are 2fold higher in microminipig microsomes than in human, dog or monkey microsomes, overview
evolution
phylogenetic analysis of the dog and human UGT1As; phylogenetic analysis of the dog and human UGT1As; phylogenetic analysis of the dog and human UGT1As; phylogenetic analysis of the dog and human UGT1As; phylogenetic analysis of the dog and human UGT1As; phylogenetic analysis of the dog and human UGT1As
evolution
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phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As; phylogenetic analysis of dog and human UGT1As
malfunction
due to frequent haplotype blocks within the UGT1 gene locus, the Gilbert variant UGT1A1*28 is often associated with polymorphisms of UGT1A6. Rare hyperserotoninemia mimicking carcinoid syndrome may be due to the linked dual polymorphisms of UGT1A1 and UGT1A6; life saving function of bilirubin glucuronidation is obvious from death of children carrying the UGT1A1-deficient Crigler-Najjar syndrome, type 1 genotype. Excessive serum bilirubin levels leading to brain damage in neonates are prevented by induction of UGT1A1, the sole enzyme conjugating bilirubin. Reduced L-thyroxine (T4)glucuronidation in carriers of the Gilbert genotype UGT1A1*28 substantiates a role for UGT1A1 in T4 glucuronidation. Due to frequent haplotype blocks within the UGT1 gene locus, the Gilbert variant UGT1A1*28 is often associated with polymorphisms of UGT1A6. Rare hyperserotoninemia mimicking carcinoid syndrome may be due to the linked dual polymorphisms of UGT1A1 and UGT1A6
malfunction
the complete absence of UGT1A1 activity results in Crigler-Najjar's syndrome type I, brain damage, and even death
metabolism
feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution; feedback loops between endobiotic UGT substrates and their transcription factors suggest an important role of their glucuronidation in evolution. AhR- and Nrf2-binding domains, termed XRE (xenobiotic responsive element) and ARE (antioxidant responsive element), respectively, are identified in the regulatory region of UGT1A1 and UGT1A6. The neurotransmitter serotonin is also solely glucuronidated by the human UGT1A6, which is highly expressed in the stomach and intestine. Serotonin exhibits a variety of functions in the gastrointestinal tract including gastrointestinal motility, mucosal growth/maintenance and intestinal inflammation
metabolism
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morphine glucuronidation and glucosidation represent complementary metabolic pathways that are both catalyzed by UDP-glucuronosyltransferase 2B7. Glucuronidation is the dominant metabolic pathway because the binding affinity of UDP-glucuronic acid to UGT2B7 is higher than that of UDPglucose. Morphine-3-beta-D-glucuronide and morphine-6-beta-D-glucuronide are the major metabolites of morphine in humans
metabolism
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as an important isoform among the UGT superfamily, the enzyme UGT2B7 is involved in the glucuronidation of many clinically important drugs
physiological function
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isoform UGT1A1 is involved in glucuronidation´of the main warfarin metabolites, including Rac-6- and 7-hydroxywarfarin and their R- and S-enantiomers in the liver
physiological function
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oxidative stress induces significant deleterious changes in astrocyte morphology, decreases cell viability and inhibits catalytic function of UDP-glucuronosyltransferases as a result of protein oxidation. Alternatively, in the surviving impaired astrocytes, oxidative conditions induces a significant overactivity and overexpression of xenobiotic detoxification enzymes, as adaptive response. These effects are significantly prevented by the presence of melatonin, reflected further on the glucuronidation activity and transcriptional regulation of both UGT1A6 and UGT1A7. Both catalytic properties of UDP-glucuronosyltransferases and the expression of UGT1A6, UGT1A7, NQO1 and NADPH:cytochrome P450 reductase in rat astrocytes are greatly influenced by the pro-oxidative environment
physiological function
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UGT2B7 is one of the most important UGTs that glucuronidates abundant endobiotics and xenobiotics, such as estriol, morphine, and anticancer drugs
physiological function
human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops. In the intestine, L-thyroxine is conjugated by UGT1A8 and UGT1A10 suggesting first-pass metabolism of oral L-thyronine, although UGT1A1 and UGT1A3 are the major UGTs glucuronidating T4 at the hydroxyl and carboxyl groups, respectively; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops. In the intestine, L-thyroxine is conjugated by UGT1A8 and UGT1A10 suggesting first-pass metabolism of oral L-thyronine, although UGT1A1 and UGT1A3 are the major UGTs glucuronidating T4 at the hydroxyl and carboxyl groups, respectively; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops, proposed feedback loop between bilirubin, AhR and AhR-controlled UGT1A1. UGT1A1 is the sole enzyme conjugating bilirubin. AhR- and Nrf2-binding domains, termed XRE (xenobiotic responsive element) and ARE (antioxidant responsive element), respectively, are identified in the regulatory region of UGT1A1 and UGT1A6; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops. The family 2 member UGT2B7 is regulated by Nrf2, but not by the AhR. UGT1A9- and UGT2B7-mediated detoxification of 20-hydroxyeicosatetraenoic acid to prevent hypertension. UGT1A9 and UGT2B7 appear to be major UGT enzymes responsible for 20-hydroxyeicosatetraenoic acid and leukotriene B4 glucuronidation; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops. UGT1A9- and UGT2B7-mediated detoxification of 20-hydroxyeicosatetraenoic acid to prevent hypertension. UGT1A9 and UGT2B7 appear to be major UGT enzymes responsible for 20-hydroxyeicosatetraenoic acid and leukotriene B4 glucuronidation; human UDP-glucuronosyltransferases are major phase II enzymes in the drug metabolism system, they also have a role in clearance and homeostasis of endogenous substrates, UGTs are often involved in detoxification of endobiotic CYP metabolites. Species- and tissue/cell-dependent regulation of UGT expression by ligand-activated transcription factors is often involved in endobiotic homeostasis. All UGT1 family members appear to be controlled by the AhR transcription factor. Bilirubin and 20-hydroxyeicosatetraenoic acid act as activators of transcription factors that regulate UGT expression, and are involved in important feedback loops. UGT2B28 is involved in estradiol and testosterone glucuronidation in a variety of tissues including breast cells
physiological function
-
glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds
physiological function
glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds; glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds; glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds; glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds; glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds
physiological function
-
glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds
physiological function
-
glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds
physiological function
-
glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds
physiological function
-
glucuronidation catalysed by UDP-glucuronosyltransferase is an important pathway in the metabolism of xenobiotics and endogenous compounds
physiological function
UDP-glucuronosyltransferase (UGT) enzymes are critical for regulating nutrients, hormones, and endobiotics, as well as for detoxifying xenobiotics. Ugt1a proteins are present and active in preimplantation murine embryos and point to a potential role for these proteins in implantation and early embryonic and fetal development.
physiological function
important role of enzyme UGT2B10 in the N-glucuronidation of drugs and other xenobiotics
physiological function
-
UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT12B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT1A9 is primarily responsible for 5-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT2B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT2B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT2B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT2B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT2B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver; UGT1A9 and 2B7 are the main contributors to regioselective glucuronidation of gingerols in the liver, isozyme UGT2B7 is primarily responsible for 4'-O-glucuronidation of gingerols in the liver
physiological function
metabolic function of UGTs can be severely influenced by hepatocellular carcinoma, analysis of alteration on the metabolism of UGTs specific substrates, translational and transcriptional activity of UGTs in hepatitis B virus-positive hepatocellular carcinoma patients, overview. In the tumor human liver microsomes, either Vmax or the clearance rates of UGT1A, UGT1A1, UGT1A4, UGT1A9 and UGT2B7 are significant lower than those of in the adjacent normal human liver microsomes. Protein and gene expressions of these isoforms are decreased in most of tumor tissues compared to the adjacent healthy tissues; metabolic function of UGTs can be severely influenced by hepatocellular carcinoma, analysis of alteration on the metabolism of UGTs specific substrates, translational and transcriptional activity of UGTs in hepatitis B virus-positive hepatocellular carcinoma patients, overview. In the tumor human liver microsomes, either Vmax or the clearance rates of UGT1A, UGT1A1, UGT1A4, UGT1A9 and UGT2B7 are significant lower than those of in the adjacent normal human liver microsomes. Protein and gene expressions of these isoforms are decreased in most of tumor tissues compared to the adjacent healthy tissues; metabolic function of UGTs can be severely influenced by hepatocellular carcinoma, analysis of alteration on the metabolism of UGTs specific substrates, translational and transcriptional activity of UGTs in hepatitis B virus-positive hepatocellular carcinoma patients, overview. In the tumor human liver microsomes, either Vmax or the clearance rates of UGT1A, UGT1A1, UGT1A4, UGT1A9 and UGT2B7 are significant lower than those of in the adjacent normal human liver microsomes. Protein and gene expressions of these isoforms are decreased in most of tumor tissues compared to the adjacent healthy tissues; metabolic function of UGTs can be severely influenced by hepatocellular carcinoma, analysis of alteration on the metabolism of UGTs specific substrates, translational and transcriptional activity of UGTs in hepatitis B virus-positive hepatocellular carcinoma patients, overview. In the tumor human liver microsomes, either Vmax or the clearance rates of UGT1A, UGT1A1, UGT1A4, UGT1A9 and UGT2B7 are significant lower than those of in the adjacent normal human liver microsomes. Protein and gene expressions of these isoforms are decreased in most of tumor tissues compared to the adjacent healthy tissues
physiological function
-
UDP-glucuronosyltransferase (UGT) enzymes are critical for regulating nutrients, hormones, and endobiotics, as well as for detoxifying xenobiotics. Ugt1a proteins are present and active in preimplantation murine embryos and point to a potential role for these proteins in implantation and early embryonic and fetal development.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+-)-11-hydroxy-DELTA9-tetrahydrocannabinol + UDP-glucuronate
? + UDP
-
substrate for isoforms UGT1A9 and UGT1A10
-
-
?
(-)-11-nor-9-carboxy-DELTA9-tetrahydrocannabinol + UDP-glucuronate
? + UDP
-
substrate for isoforms UGT1A1 and UGT1A3, no substrate for UGT1A9 and UGT1A10
-
-
?
(-)-borneol + UDP-glucuronate
UDP + (-)-borneol-O-alpha-D-glucuronide
-
-
-
?
(R)-6-hydroxywarfarin + UDP-alpha-D-glucuronate
(R)-6-hydroxywarfarin 6-O-beta-D-glucuronide + UDP
-
-
-
-
?
(R)-7-hydroxywarfarin + UDP-alpha-D-glucuronate
(R)-7-hydroxywarfarin 7-O-beta-D-glucuronide + UDP
-
-
-
-
?
(R)-8-hydroxywarfarin + UDP-alpha-D-glucuronate
(R)-8-hydroxywarfarin 8-O-beta-D-glucuronide + UDP
-
-
-
-
?
(S)-6-hydroxywarfarin + UDP-alpha-D-glucuronate
(S)-6-hydroxywarfarin 6-O-beta-D-glucuronide + UDP
-
-
-
-
?
(S)-7-hydroxywarfarin + UDP-alpha-D-glucuronate
(S)-7-hydroxywarfarin 7-O-beta-D-glucuronide + UDP
-
-
-
-
?
(S)-8-hydroxywarfarin + UDP-alpha-D-glucuronate
(S)-8-hydroxywarfarin 8-O-beta-D-glucuronide + UDP
-
-
-
-
?
(S)-naproxen + UDP-alpha-D-glucuronate
beta-D-glucuronosyl (S)-naproxen + UDP
-
-
-
-
?
(S)-naproxen + UDP-alpha-D-glucuronate
UDP + beta-D-glucuronosyl (S)-naproxen
-
-
-
-
?
1-hydroxy-benzo(a)pyrene + UDP-glucuronate
1-hydroxy-benzo(a)pyrene 1-O-glucuronate + UDP
-
-
-
-
?
1-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-1-yl-beta-D-glucuronide
-
-
-
?
1-hydroxypyrene + UDP-glucuronate
1-hydroxypyrene 1-O-glucuronate + UDP
-
-
-
-
?
1-hydroxy[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-1-yl-alpha-D-glucuronide
-
-
-
-
?
1-naphthol + UDP-alpha-D-glucuronate
1-naphthyl O-glucuronide + UDP
-
-
-
-
?
1-naphthol + UDP-glucuronate
1-naphthyl-O-glucuronide + UDP
-
-
-
?
10-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-10-yl-beta-D-glucuronide
-
-
-
?
11-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-11-yl-beta-D-glucuronide
-
-
-
?
11alpha-hydroxyprogesterone + UDP-glucuronate
UDP + 11alpha-hydroxyprogesterone-11-O-alpha-D-glucuronate
-
-
-
?
12-hydroxyeicosatetraenoic acid + UDP-glucuronate
?
-
-
-
?
13-hydroxyoctadecadienoic acid + UDP-glucuronate
?
-
-
-
?
16alpha-hydroxyprogesterone + UDP-glucuronate
UDP + 16alpha-hydroxyprgesterone-16-O-alpha-D-glucuronate
UGT2B15 and UGT2B17 are the major enzyme forms involved in the high-affinity component of 16alpha-hydroxyprogesterone glucuronidation
-
-
?
16alpha-hydroxyprogesterone + UDP-glucuronate
UDP + 16alpha-hydroxyprogesteron-16-O-alpha-D-glucuronate
-
-
-
?
17alpha-ethynylestradiol + UDP-glucuronate
UDP + 17alpha-ethynylestradiol 3-O-beta-D-glucuronide
-
-
-
?
17beta-hydroxy-5alpha-androstan-3-one + UDPglucuronate
UDP + 17beta-hydroxy-5alpha-androstan-3-one 17O-glucuronide
-
-
-
?
2 UDP-D-glucuronate + 2 dexmedetomidine
2 UDP + dexmedetomidine N1-beta-D-glucuronoside + dexmedetomidine N3-beta-D-glucuronoside
2 UDP-D-glucuronate + 2 levomedetomidine
2 UDP + levomedetomidine N1-beta-D-glucuronoside + dexmedetomidine N3-beta-D-glucuronoside
2',4,4'-trihydroxychalcone + UDP-glucuronate
UDP + 2',4,4'-trihydroxychalcone 4'-O-glucoside + 2',4,4'-trihydroxychalcone 2'-O-glucoside
-
i.e. isoliquiritigenin
-
-
?
2-(4-chlorophenyl)-5-(2-furyl)-4-oxazoleacetic acid + UDPglucuronate
?
-
glucuronidation of 2-(4-chlorophenyl)-5-(2-furyl)-4-oxazoleacetic acid is mainly catalyzed by UGT1A1, UGT1A9, and UGT2B7 in the liver, and by UGT1A1, UGT1A3, and UGT2B7 in the intestine in humans
-
-
?
2-hydroxy-2',3',4',5'-tetrachlorobiphenyl + UDPglucuronate
UDP + 2',3',4',5'-tetrachlorobiphenyl 2-O-glucuronate
-
-
-
?
2-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-2-yl-beta-D-glucuronide
-
-
-
?
2-methoxy-4-(2-propenyl)phenol + UDPglucuronate
UDP + 2-methoxy-4-(2-propenyl)phenylglucuronide
21-hydroxyprogesterone + UDP-glucuronate
UDP + 21-hydroxyprogesterone-21-O-alpha-D-glucuronate
-
-
-
?
3'-azido-3'-deoxythymidine + UDP-alpha-D-glucuronate
3'-azido-3'-deoxythymidine 5'-O-glucuronide + UDP
-
substrate of isoform UGT2B7
-
-
?
3'-azido-3'-deoxythymidine + UDPglucuronate
3'-azido-3'-deoxythymidine 5'-O-glucuronide + UDP
3-hydroxy-benzo(a)pyrene + UDP-glucuronate
3-hydroxy-benzo(a)pyrene 3-O-glucuronate + UDP
-
-
-
-
?
3-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-3-yl-beta-D-glucuronide
-
-
-
?
4-aminobiphenyl + UDPglucuronate
UDP + ?
-
catalyzed by isozyme 1 but not by isozyme 2
-
-
?
4-hydroxy-2',3,3',4',5'-pentachlorobiphenyl + UDPglucuronate
UDP + 2,3,3',4',5'-pentachlorobiphenyl 4-O-glucuronate
-
-
-
?
4-hydroxy-2',3,3',4',5,5'-heptachlorobiphenyl + UDPglucuronate
UDP + 2',3,3',4',5,5'-hexachlorobiphenyl 4-O-glucuronate
-
-
-
?
4-hydroxy-2',3,4',5,6'-pentachlorobiphenyl + UDPglucuronate
UDP + 2',3,4',5,6'-pentachlorobiphenyl 4-O-glucuronate
-
-
-
?
4-hydroxy-2',3,4',6'-tetrachlorobiphenyl + UDP-glucuronate
UDP + 2',4',6'-trichlorobiphenyl 4-O-glucuronate
-
-
-
?
4-hydroxy-2',4',6'-trichlorobiphenyl + UDP-glucuronate
UDP + 2',4',6'-trichlorobiphenyl 4-O-glucuronate
-
-
-
?
4-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-4-yl-beta-D-glucuronide
-
-
-
?
4-hydroxyestrone + UDP-glucuronate
UDP + 4-hydroxyestrone-4-O-beta-D-glucuronide
-
-
-
-
?
4-methylumbeliferone + UDP-alpha-D-glucuronate
4-methylumbelliferyl-7-O-alpha-D-glucuronide
-
-
-
-
?
4-methylumbeliferone + UDP-glucuronate
4-methylumbelliferyl-7-O-beta-D-glucuronide
-
-
-
?
4-methylumbelliferone + UDP-glucuronate
UDP + 4-methylumbelliferyl-7-O-beta-D-glucuronide
4-n-octylgallate + UDPglucuronate
UDP + 4-n-octylgallate 3-O-glucuronide
-
highly specific for UGT1A71
-
?
5-diethylaminoethylamino-8-hydroxyimidazoacridinone + UDP-alpha-D-glucuronate
5-{[2-(diethylamino)ethyl]amino}-6-oxo-6H-imidazo[4,5,1-de]acridin-8-yl beta-D-glucuronide + UDP
-
i.e. antitumor agent C-1311, NSC-645809
-
-
?
5-dimethylaminopropylamino-8-hydroxytriazoloacridinone + UDP-alpha-D-glucuronate
5-dimethylaminopropylamino-8-hydroxytriazoloacridinone-8-D-glucuronide + UDP
-
i.e. antitumor agent C-1305
-
-
?
5-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-5-yl-beta-D-glucuronide
-
-
-
?
5-hydroxybenzo[a]pyrene + UDPglucuronate
UDP + 5-hydroxybenzo[a]pyrene O-glucuronide
-
glucuronidated by UGT1A3
-
?
5alpha-androstane-3alpha,17beta-diol + UDP-glucuronate
?
-
-
-
?
5alpha-androstane-3alpha,17beta-diol + UDP-glucuronate
UDP + 5alpha-androstane-3alpha,17beta-diol O-glucuronide
5beta-androstane-3alpha,17beta-diol + UDP-glucuronate
UDP + 5beta-androstane-3alpha,17beta-diol O-glucuronide
-
-
-
?
6-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-6-yl-beta-D-glucuronide
-
-
-
?
6alpha-hydroxyprogesterone + UDP-glucuronate
UDP + 6alpha-hydroxyprogesteron-6-O-alpha-D-glucuronate
-
-
-
?
7,7,7-triphenylheptanoic acid + UDPglucuronate
UDP + 7,7,7-triphenylheptanoic acid glucuronide
7-ethyl-10-hydroxy-camptothecin carboxylate + UDP-glucuronate
UDP + 7-ethyl-camptothecin carboxylate-10-yl-beta-D-glucuronate
7-ethyl-10-hydroxy-camptothecin lactone + UDP-glucuronate
UDP + 7-ethyl-camptothecin lactone-10-yl-beta-D-glucuronate
7-ethyl-10-hydroxycamptothecin + UDP-alpha-D-glucuronate
7-ethyl-10-hydroxycamptothecin 10-O-glucuronate + UDP
7-hydroxy-4-(trifluoromethyl)-coumarin + UDPglucuronate
UDP + 7-hydroxy-4-(trifluoromethyl)-coumarin O-glucuronide
-
-
-
?
7-hydroxy-4-trifluoromethylcoumarin + UDP-alpha-D-glucuronate
7-hydroxy-4-trifluoromethylcoumarin 7-O-glucuronate + UDP
7-hydroxy-benzo(a)pyrene + UDP-glucuronate
7-hydroxy-benzo(a)pyrene 7-O-glucuronate + UDP
-
-
-
-
?
7-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-7-yl-beta-D-glucuronide
-
-
-
?
7-hydroxycoumarin + UDP-glucuronate
UDP + coumarin-7-yl-alpha-D-glucuronide
-
-
-
?
8-hydroxy-benzo(a)pyrene + UDP-glucuronate
8-hydroxy-benzo(a)pyrene 8-O-glucuronate + UDP
-
-
-
-
?
8-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-8-yl-beta-D-glucuronide
-
-
-
?
8-hydroxyquinoline + UDPglucuronate
UDP + 8-hydroxyquinoline 8-O-glucuronide
-
-
-
?
9-hydroxybenzo[a]pyrene + UDP-glucuronate
UDP + benzo[a]pyren-9-yl-beta-D-glucuronide
-
-
-
?
androstane-3alpha,17beta diol + UDPglucuronate
UDP + androstane-3alpha,17beta diol O-glucuronide
-
-
-
?
benzo[a]pyrene 3,6-diphenol + UDP-glucuronate
?
-
converted readily to mono- and diglucuronides
-
-
?
benzo[a]pyrene 3,6-quinone + UDPglucuronate
benzo[a]pyrene 3,6-quinol glucuronide + UDP
-
-
no information to which positions 3-, 6-, or both the glucuronate is attached
?
benzo[a]pyrene-3,6-quinol + UDPglucuronate
benzo[a]pyrene 3,6-quinol mono- and diglucuronide + UDP
-
-
-
?
beta-estradiol + UDP-alpha-D-glucuronate
beta-estradiol-3-glucuronide + UDP
-
-
-
-
?
bilirubin + UDP-glucuronate
bilirubin glucuronoside + UDP
-
UGT1A1 exhibits the highest tranilast glucuronosyltransferase activity (13.5 pmol/min/mg protein)
-
-
?
cannabinol + UDP-glucuronate
? + UDP
-
substrate for hepatic isoform UGT1A9 and extrahepatic UGT1A7, UGT1A8, and UGT1A10
-
-
?
carvacrol + UDP-glucuronate
caervcrol O-glucuronate + UDP
-
isoform UGT1A9 is the major isozyme responsible for glucuronidation in liver microsomes, and isoform UGT1A7 plays a major role for glucuronidation in intestinal microsomes
-
-
?
chenodeoxycholic acid + UDPgalacturonate
UDP + chenodeoxycholic acid O-galacturonide
-
-
-
?
codeine + UDPglucuronate
codeine-6-glucuronide + UDP
-
glucuronidated by HGT2B7H and HGT2B7Y
-
-
deoxycholic acid + UDPglucuronate
UDP + deoxycholic acid O-glucuronide
-
-
-
?
digitoxigenin + UDPglucuronate
UDP + digitoxigenin O-glucuronide
-
-
-
?
dihydromorphine + UDPglucuronate
UDP + dihydromorphine O-glucuronide
-
-
-
?
dihydromorphone + UDPglucuronate
UDP + dihydromorphone O-glucuronide
-
-
-
?
dihydrotestosterone + UDP-alpha-D-glucuronate
dihydrotestosterone D-glucuronate + UDP
-
-
-
-
?
dihydrotestosterone + UDPglucuronate
UDP + dihydrotestosterone O-glucuronide
-
-
-
?
edaravone + UDP-alpha-D-glucuronate
edaravone beta-D-glucuronate + UDP
-
i.e. 3-methyl-1-phenyl-2-pyrazolin-5-one. Edaravone glucuronidation in liver microsomes and kidney microsomes exhibits biphasic kinetics. UDP glucuronosyltransferases UGT1A1, UGT1A6, UGT1A7, UGT1A8, UGT1A9, UGT1A10, UGT2B7, and UGT2B17 produce a significant amount of glucuronide metabolite. Among them, UGT1A9 exhibits the highest activity, followed by UGT2B17 and UGT1A7
-
-
?
epitestosterone + UDP-glucuronate
UDP + epitestosterone O-glucuronide
-
glucuronidated by HGT2B7H and HGT2B7Y
-
?
estradiol + UDP-alpha-D-glucuronate
estradiol 3-O-glucuronate + UDP
sigmoidal kinetics with n of 1.7
-
-
?
estradiol + UDP-alpha-D-glucuronate
UDP + estradiol 3-O-glucuronide
-
substrate of isoform UGT1A1
-
-
?
estradiol + UDP-glucuronate
estradiol 3-O-glucuronate + UDP
sigmoidal kinetics with n of 1.7
-
-
?
estradiol-17alpha + UDPglucuronate
UDP + 17-alpha-estradiol O-glucuronide
-
-
-
?
ethinylestradiol + UDPglucuronate
UDP + ethinylestradiol-3-glucuronide
-
-
-
?
flurbiprofen + UDP-glucuronate
?
-
metabilized by mutant enzyme S432G-UGT1A7, but not by wild-type enzyme UGT1A7
-
-
?
glycolithocholic acid + UDPglucuronate
UDP + glycolithocholic acid O-glucuronide
-
lowest activity among five bile acids studied
-
?
morphine + UDP-glucuronate
UDP + morphine 3-glucuronide + morphine 6-glucuronide
-
-
-
-
?
mycophenolic acid + UDP-alpha-D-glucuronate
mycophenolic acid D-glucuronide
-
-
-
-
?
N-hydroxy-2-acetylaminofluorene + UDPglucuronate
UDP + N-hydroxy-2-acetylaminofluorene O-glucuronide
-
glucuronidated by UGT1A3 in preference to the ring-hydroxylated derivatives
-
?
nalorphine + UDPglucuronate
UDP + nalorphine O-glucuronate
-
-
-
?
naltrexone + UDPglucuronate
UDP + naltrexone O-glucuronide
-
-
-
?
opiates + UDPglucuronate
opiates 6-O-glucuronides + UDP
-
substrate for UGT2B7
-
-
oxymorphone + UDPglucuronate
UDP + oxymorphone O-glucuronide
-
-
-
?
planar phenols + UDPglucuronate
UDP + phenylglucuronides
-
expressed before birth
-
-
-
propofol + UDP-alpha-D-glucuronate
UDP + estradiol O-glucuronide
-
substrate of isoform UGT1A9
-
-
?
propofol + UDP-glucuronate
UDP + propofyl beta-D-glucuronide
-
-
-
?
scopoletin + UDP-glucuronate
UDP + scopoletin O-glucoside
very low rate of glucuronidation
-
-
?
senecionine + UDP-alpha-D-glucuronate
senecionine N-glucuronide + UDP
-
senecionine is a representative of the hepatotoxic pyrrolizidine alkaloids. Glucuronidation is mediated by isofrom UGT1A4 and follows typical Michaelis-Menten kinetics
-
-
?
testosterone + UDP-glucuronate
UDP + testosterone 17-O-glucuronide
-
isoform UGT2B17 is the most active enzyme in testosterone glucuronidation. Isoform UGT2A1, an extrahepatic enzyme that is expressed mainly in the nasal epithelium, catalyzes the glucuronidation of both steroids at considerable rates and similar kinetics
-
-
?
testosterone + UDP-glucuronate
UDP + testosterone-17-O-alpha-D-glucuronate
-
-
-
?
testosterone + UDP-glucuronate
UDP + testosterone-17alpha-glucuronide
-
-
-
?
trans-androsterone + UDP-alpha-D-glucuronate
trans-androsterone D-glucuronate + UDP
-
-
-
-
?
trifluoperazine + UDP-glucuronate
UDP + ?
-
substrate for isoform UGT1A4 and isoform UGT1A1 mutant H39P
-
-
?
UDP-alpha-D-glucuronate + 3-hydroxyflavone
UDP + 3-[(beta-D-glucopyranurnosyl)oxy]-flavone
isozyme UGT1A1
-
-
?
UDP-alpha-D-glucuronate + diclofenac
UDP + diclofenac O-beta-D-glucuronide
-
-
-
?
UDP-alpha-D-glucuronate + dopamine
UDP + dopamine 3-O-beta-D-glucopyranosiduronic acid
-
substrate for isoform UGT1A10, no substrate for all other UGT enzymes tested
-
-
?
UDP-alpha-D-glucuronate + dopamine
UDP + dopamine 4-O-beta-D-glucopyranosiduronic acid
-
-
substrate for isoform UGT1A10, no substrate for all other UGT enzymes tested
-
?
UDP-alpha-glucuronate + diclofenac
UDP + beta-D-glucuronosyl-diclofenac
-
-
-
-
?
UDP-D-glucuronate + 11alpha-hydroxyprogesterone
UDP + 11alpha-hydroxyprogesterone 11-O-beta-D-glucuronoside
an UGT2B7 substrate
-
-
?
UDP-D-glucuronate + 17beta-estradiol
UDP + 17beta-estradiol 3-O-beta-D-glucuronoside
-
-
-
?
UDP-D-glucuronate + 17beta-estradiol
UDP + 17beta-estradiol-3-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + 1alpha,25-dihydroxyvitamin D3
UDP + 1alpha,25-dihydroxyvitamin D3 25-O-beta-D-glucuronoside
among 12 different UGT isozymes tested, only UGT1A4, and also UGT2B4 and UGT2B7 support the reaction, the main product by UGT1A4 supersomes and human liver microsomes is the 25-O-glucuronide, product identification and determination by mass spectral and NMR analyses, overview
-
-
?
UDP-D-glucuronate + 2-hydroxyestradiol
UDP + 2-hydroxyestradiol beta-D-glucuronoside
isozyme UGT1A1
-
-
?
UDP-D-glucuronate + 2-hydroxyestrone
UDP + 2-hydroxyestrone beta-D-glucuronoside
isozyme UGT1A1
-
-
?
UDP-D-glucuronate + 3'-azido-3'-deoxythymidine
UDP + 3'-azido-3'-deoxythymidine 5'-O-beta-D-glucuronoside
model substrate for determination of glucuronidation with respect to specificity, linearity, detection limit, recovery, stability, precision and accuracy, method development and validation for assay and chromatographic determination of reaction products, overview
-
-
?
UDP-D-glucuronate + 3-hydroxydesloratadine
UDP + 3-hydroxydesloratadine beta-O-D-glucuronoside
-
specific substrate of isozyme UGT1A8
-
-
?
UDP-D-glucuronate + 4'-hydroxy-warfarin
UDP + 4'-hydroxy-warfarin beta-D-glucuronoside
substrate of isozyme UGT1A10
-
-
?
UDP-D-glucuronate + 4-(trifluoromethyl)-umbelliferone
UDP + 4-(trifluoromethyl)-umbelliferone beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + 4-hydroxy-N-desmethyl-tamoxifen
UDP + 4-hydroxy-N-desmethyl-tamoxifen beta-D-glucuronoside
UDP-D-glucuronate + 4-methylumbelliferone
UDP + 4-methylumbelliferone beta-D-glucuronoside
UDP-D-glucuronate + 4-methylumbelliferone
UDP + 4-methylumbelliferonyl beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + 4-methylumbelliferone
UDP + 4-methylumbelliferyl beta-O-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + 4-nitrophenol
UDP + 4-nitrophenyl beta-O-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + apigenin
UDP + apigenin 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + beta-D-estradiol
UDP + beta-estradiol 3-O-beta-D-glucuronoside
isozyme UGT1A1
-
-
?
UDP-D-glucuronate + beta-estradiol
UDP + beta-estradiol 3-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + bilirubin
UDP + bilirubin beta-D-glucuronoside
isozyme UGT1A1
-
-
?
UDP-D-glucuronate + bisdemethoxy-curcumin
UDP + bisdemethoxy-curcumin phenolic beta-D-monoglucuronide
-
-
-
-
?
UDP-D-glucuronate + candesartan
UDP + candesartan beta-D-glucuronoside
-
isozyme UGT1A3 exhibites a strong regioselectivity towards the N2 position of the tetrazole ring, also isozyme UGT2B7 glucuronidates candesartan at the tetrazole-N2 position, whereas isozymes UGT1A7, UGT1A8, UGT1A9, and UGT1A10 mainly yield candesartan O-glucuronide
-
-
?
UDP-D-glucuronate + chenodeoxycholic acid
UDP + hyodeoxycholic acid 6-O-glucuronoside
isozyme UGT2A3
-
-
?
UDP-D-glucuronate + curcumin
UDP + curcumin beta-D-glucuronoside
-
low activity, can reverse the inhibtory effect of curcumin on UGTs
-
-
?
UDP-D-glucuronate + dehydrotestosterone
UDP + dehydrotestosterone 17-O-beta-D-glucuronoside
UDP-D-glucuronate + demethoxy-curcumin
UDP + demethoxy-curcumin phenolic beta-D-monoglucuronide
-
-
-
-
?
UDP-D-glucuronate + deoxycholic acid
UDP + hyodeoxycholic acid 6-O-glucuronoside
isozyme UGT2A3
-
-
?
UDP-D-glucuronate + dihydrotestosterone
UDP + dihydrotestosterone 17-O-beta-D-glucuronoside
UDP-D-glucuronate + eriodictyol
UDP + eriodictyol 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + flurbiprofen
UDP + flurbiprofen beta-D-glucuronoside
-
isozyme UGT2B7
-
-
?
UDP-D-glucuronate + hesperetin
UDP + hesperetin 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + homoeriodictyol
UDP + homoeriodictyol 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + hyodeoxycholic acid
UDP + hyodeoxycholic acid 24-carboxy-glucuronoside
recombinant enzyme, expressed in insect cells via baculovirus system, selective glucuronidation
product formation depends on the isozyme, overview
-
?
UDP-D-glucuronate + hyodeoxycholic acid
UDP + hyodeoxycholic acid 3-O-glucuronoside
recombinant enzyme, expressed in insect cells via baculovirus system, selective glucuronidation
product formation depends on the isozyme, overview
-
?
UDP-D-glucuronate + imipramine
UDP + imipramine N-beta-D-glucuronoside
-
reaction of isozyme UGT1A4
-
-
?
UDP-D-glucuronate + isolongifolol
UDP + isolongifolol beta-D-glucuronoside
-
the compound is substrate and competitive inhibitor
-
-
?
UDP-D-glucuronate + kaempferol
UDP + kaempferol 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + longifolol
UDP + longifolol beta-D-glucuronoside
-
the compound is substrate and competitive inhibitor
-
-
?
UDP-D-glucuronate + losartan
UDP + losartan beta-D-glucuronoside
-
no O-glucuronide is generated by any isozyme, while isozymes UGT1A1, UGT1A3, 1A10, UGT2B7, and UGT2B17 glucuronidate losartan at the tetrazole-N2, isozyme UGT1A10 also yields the respective N1-glucuronide, isozyme UGT1A3 exhibites a strong regioselectivity towards the N2 position of the tetrazole ring
-
-
?
UDP-D-glucuronate + menadiol
UDP + mendadiol 1-O-beta-D-glucuronoside
-
-
isoform UGT1A6, formation of 1-menadiol glucuronide and 4-menadiol glucuronide in ratio of about 4:1
-
?
UDP-D-glucuronate + menadiol
UDP + mendadiol 4-O-beta-D-glucuronoside
-
-
isoform UGT1A10, preferential formation of 4-menadiol glucuronoside, isoform UGT1A6, formation of 1-menadiol glucuronide and 4-menadiol glucuronide in ratio of about 4:1
-
?
UDP-D-glucuronate + morphine
UDP + morphine 3-beta-D-glucuronoside
-
activity of isozyme UGT1A8
-
-
?
UDP-D-glucuronate + morphine
UDP + morphine 6-O-beta-D-glucuronoside
-
-
-
?
UDP-D-glucuronate + mycophenolic acid
UDP + mycophenolic acid beta-D-glucuronoside
-
K314 and K404m are determined binding sites required for UDP-glcA binding to isozyme UGT1A10, overview
-
-
?
UDP-D-glucuronate + myricetin
UDP + myricetin 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + naringenin
UDP + naringenin 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + phenolphthalein
UDP + phenolphthalein beta-D-glucuronoside
an UGT2B15 substrate
-
-
?
UDP-D-glucuronate + phenolphthalein
UDP + phenolphthalein beta-D-monoglucuronoside
-
-
-
-
?
UDP-D-glucuronate + quercetin
UDP + quercetin 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + serotonin
UDP + serotonin beta-D-glucuronoside
isozyme UGT1A6
-
-
?
UDP-D-glucuronate + serotonin
UDP + serotonin O-beta-D-glucuronoside
-
reaction of isozyme UGT1A6
-
-
?
UDP-D-glucuronate + testosterone
UDP + testosterone 17-O-beta-D-glucuronoside
an UGT2B15 substrate
-
-
?
UDP-D-glucuronate + trans-4-hydroxytamoxifen
UDP + 4-hydroxytamoxifen beta-D-glucuronoside
UDP-D-glucuronate + trifluoperazine
UDP + trifluoperazine beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + umbelliferone
UDP + umbelliferyl beta-D-glucuronoside
-
-
-
-
?
UDP-D-glucuronate + ursodeoxycholic acid
UDP + hyodeoxycholic acid 6-O-glucuronoside
isozyme UGT2A3
-
-
?
UDP-D-glucuronate + zolarsartan
UDP + zolarsartan beta-D-glucuronoside
-
isozyme UGT1A3 exhibites a strong regioselectivity towards the N2 position of the tetrazole ring, the tetrazole-N1 of this aglycone is accessible to other enzymes, including isozyme UGT1A5, zolarsartan O-glucuronide is mainly produced by isozyme UGT1A10 and isozyme UGT2B7
-
-
?
UDP-glucuronate + (E)-2,4-dimethoxy-6-(4-methoxystyryl)benzaldehyde oxime
UDP + 1-O-[(Z)-(2,4-dimethoxy-6[(E)-2-(4-methoxyphenyl)ethenyl]methylidene)amino]-beta-D-glucuronate
UDP-glucuronate + (E)-3-(3-hydroxy-4-methoxyphenyl)-2-(3,4,5-trimethoxyphenyl)acrylic acid
UDP + ?
-
i.e. NI-12a, low activity, NI-12a is glucuronidated at both the -COOH and -OH functions. NI-12a is primarily metabolized by the hepatic and renal enzyme UGT1A9
-
-
?
UDP-glucuronate + 1,25-dihydroxyergocalciferol
UDP + 1,25-dihydroxyergocalciferol beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 1-hydroxypyrene
UDP + 1-hydroxypyrene beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 10-gingerol
UDP + 10-gingerol 4'-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 10-gingerol
UDP + 10-gingerol 5-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 10-gingerol
UDP + 6-gingerol 5-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 12-hydroxyeicosatetraenoic acid
UDP + 12-hydroxyeicosatetraenoyl beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 12-hydroxyeicosatetraenoic acid
UDP + 12-hydroxyeicosatetraenoyl-beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 15-hydroxyeicosatetraenoic acid
UDP + 15-hydroxyeicosatetraenoyl beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 15-hydroxyeicosatetraenoic acid
UDP + 15-hydroxyeicosatetraenoyl-beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 17beta-estradiol
UDP + 17beta-estradiol 3-O-glucuronide
-
-
-
?
UDP-glucuronate + 17beta-estradiol
UDP + estradiol 17-beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 2',4'-hydroxychalcone
UDP + 2'-hydroxychalcone 4'-O-beta-D-glucuronoside
-
glucuronidation at the OH-4' position by UGT1A1 and UGT1A10 isoforms, both UGT1A6 and 1A9 produced two chalcone monoglucuronides, the 4'-Oglucuronide and the 2'-O-glucuronide
-
-
?
UDP-glucuronate + 2',4'-hydroxychalcone
UDP + 4'-hydroxychalcone 2'-O-beta-D-glucuronoside
-
glucuronidation at the OH-2' position with low activity by UGT1A7, UGT1A6, and UGT1A10 isoforms, and with high activity by isozyme UGT1A9. Both UGT1A6 and 1A9 produced two chalcone monoglucuronides, the 4'-Oglucuronide and the 2'-O-glucuronide
-
-
?
UDP-glucuronate + 2'-hydroxychalcone
UDP + chalcone 2'-O-beta-D-glucuronoside
-
glucuronidation at the OH-2' position by UGT1A9 isoform
-
-
?
UDP-glucuronate + 2-hydroxyestrone
UDP + 2-hydroxyestrone beta-D-glucuronide
-
-
-
-
?
UDP-glucuronate + 2-methoxyestrone
UDP + 2-methoxyestrone beta-D-glucuronide
-
-
-
-
?
UDP-glucuronate + 20-hydroxyeicosatetraenoic acid
UDP + 20-hydroxyeicosatetraenoyl beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 25-hydroxyergocalciferol
UDP + 25-hydroxyergocalciferol beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 3'-azido-3'-deoxythymidine
UDP + 3'-azido-3'-deoxythymidine beta-D-glucuronide
-
isozymes UGT2B4, UGT2B7, and UGT2B17
-
-
?
UDP-glucuronate + 3'-azido-3'-deoxythymidine
UDP + 3'-azido-3'-deoxythymidine beta-D-glucuronoside
UDP-glucuronate + 3,17-estradiol
UDP + 17-estradiol 3-O-glucuronide
-
isozyme UGT1A1
-
-
?
UDP-glucuronate + 3,17-estradiol
UDP + 3-estradiol 17-O-glucuronide
-
isozyme UGT1A1
-
-
?
UDP-glucuronate + 3,2'-dihydroxychalcone
UDP + 3-hydroxychalcone 2'-O-beta-D-glucuronoside
-
very low activity with isozyme UGT1A6
-
-
?
UDP-glucuronate + 3,2'-hydroxychalcone
UDP + 3-hydroxychalcone 2'-O-beta-D-glucuronoside
-
glucuronidation at the OH-2' position by UGT1A8 isoform
-
-
?
UDP-glucuronate + 3-epideacetycinobufagin
UDP + 3-epideacetycinobufagin 3-beta-D-glucuronoside
UDP-glucuronate + 3alpha,5beta-tetrahydroaldosterone
UDP + 3alpha,5beta-tetrahydroaldosterone beta-D-glucuronide
high activity
-
-
?
UDP-glucuronate + 4,2'-hydroxychalcone
UDP + 4-hydroxychalcone 2'-O-beta-D-glucuronoside
-
glucuronidation at the OH-2' position by UGT1A8, UGT1A1, and UGT1A3 isoforms. The A-ring OH-4 group promotes glucuronidation at the 2' position for the reaction of the exclusive substrate 4,2'-dihydroxychalcone of UGT1A1 and 1A3
-
-
?
UDP-glucuronate + 4-hydroxy-estrone
UDP + ?
glucuronidation of 4-hydroxylated estrone is significantly reduced in breast carcinomas compared to healthy
-
-
?
UDP-glucuronate + 4-hydroxyestradiol
UDP + 4-hydroxyestradiol beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 4-hydroxyretinoic acid
UDP + 4-hydroxyretinoic acid beta-D-glucuronoside
mainly conjugated by UGT2B7
-
-
?
UDP-glucuronate + 4-methoxyestrone
UDP + 4-methoxyestrone beta-D-glucuronide
-
-
-
-
?
UDP-glucuronate + 4-methylumbelliferone
UDP + 4-methylumbelliferyl-beta-D-glucuronide
-
all isozymes, nonselective substrate
-
-
?
UDP-glucuronate + 4-methylumbelliferone
UDP + 4-methylumbelliferyl-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 4-nitrophenol
UDP + 4-nitrophenol beta-D-glucuronide
-
-
-
-
?
UDP-glucuronate + 5-hydroxytryptophol
UDP + 5-hydroxy-tryptophol beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + 5-hydroxytryptophol
UDP + 5-hydroxytryptophol beta-D-glucuronide
isozymes UGT1A6 and UGT1A9, the latter shows over 20fold lower activity
-
-
?
UDP-glucuronate + 5-hydroxytryptophol
UDP + 5-hydroxytryptophol beta-D-glucuronoside
mucosal serotonin and its metabolite 5-hydroxytryptophol are solely conjugated by UGT1A6
-
-
?
UDP-glucuronate + 5alpha-dihydroaldosterone
UDP + 5alpha-dihydroaldosterone beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 5alpha-tetrahydrocortisone
UDP + 5alpha-tetrahydrocortisone beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 5beta-tetrahydrocortisone
UDP + 5beta-tetrahydrocortisone beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 6-gingerol
UDP + 6-gingerol 4'-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 6-gingerol
UDP + 6-gingerol 5-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 6-hydroxymelatonin
UDP + 6-hydroxymelatonin beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 7-ethyl-10-hydroxy-camptothecin
UDP + 7-ethyl-10-hydroxy-camptothecin beta-D-glucuronoside
i.e. SN-38, an active metabolite of irinotecan
-
-
?
UDP-glucuronate + 7-ethyl-10-hydroxycampothecin
UDP + 7-ethyl-10-hydroxycampothecin 1-O-beta-D-glucuronide
i.e. SN-38, isozymes UGT1A1, UGT1A7, and UGT1A9
-
-
?
UDP-glucuronate + 7-ethyl-10-hydroxycamptothecin
UDP + 7-ethyl-10-hydroxycamptothecin 10-O-beta-D-glucuronoside
i.e. SN-38, an active metabolite of irinotecan
-
-
?
UDP-glucuronate + 7-hydroxy-4-trifluoromethylcoumarin
UDP + 4-trifluoromethylcoumarin 7-O-beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 7-hydroxy-4-trifluoromethylcoumarin
UDP + 7-hydroxy-4-trifluoromethylcoumarin beta-D-glucuronide
-
-
-
?
UDP-glucuronate + 7-hydroxyflavanone
UDP + flavanone 7-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 8-gingerol
UDP + 6-gingerol 5-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 8-gingerol
UDP + 8-gingerol 4'-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 8-gingerol
UDP + 8-gingerol 5-O-beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + 8-hydroxyquinoline
UDP + 8-hydroxyquinoline beta-D-glucuronide
-
-
-
?
UDP-glucuronate + aldosterone
UDP + aldosterone beta-D-glucuronide
-
-
-
?
UDP-glucuronate + all-trans-retinoic acid
UDP + all-trans-retinoic acid beta-D-glucuronoside
mainly conjugated by UGT2B7
-
-
?
UDP-glucuronate + Aloe-emodin
UDP + Aloe-emodin beta-D-glucuronide
isozyme UGT1A7
-
-
?
UDP-glucuronate + amitriptyline
UDP + amitriptyline beta-D-glucuronoside
-
-
-
-
?
UDP-glucuronate + amitryptiline
UDP + amitryptiline beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + androstane-3,17-diol
UDP + androstane-3,17-diol 17-O-beta-D-glucuronide
-
isozyme UGT2B15
-
-
?
UDP-glucuronate + androstanediol
UDP + androstanediol beta-D-glucuronoside
-
-
-
?
UDP-glucuronate + anthraflavic acid
UDP + anthraflavic acid 2-glucuronide
-
isozyme UGT1A1
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-
?
UDP-glucuronate + asialo-orosomucoid
UDP + asialo-orosomucoid beta-D-glucuronide
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acceptor is a glycoprotein, preferred substrate
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-
?
UDP-glucuronate + cardamonin
UDP + cardamonin beta-D-glucuronoside
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UGT1A9 is the only isoform to glucuronidate cardamonin at the OH-2' position, lower activity with isozyme UGT1A7
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?