Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Human UGT2B7 catalyzes morphine glucuronidation

B L Coffman1, G R Rios, C D King

  • 1Department of Pharmacology, University of Iowa, Iowa City 52242, USA.

Drug Metabolism and Disposition: the Biological Fate of Chemicals
|January 1, 1997
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cross-sectional and within-person associations of chronic overlapping pain conditions and psychosocial functioning in young adults.

The journal of pain·2026
Same author

Modifications to the gut microbiome alter bone matrix proteomics and fracture toughness at the cellular scale.

bioRxiv : the preprint server for biology·2025
Same author

Reply to: Interindividual differences in pain can be explained by fMRI, sociodemographic, and psychological factors.

Nature communications·2024
Same author

Denoising task-related fMRI: Balancing noise reduction against signal loss.

Human brain mapping·2023
Same author

β-hydroxybutyrate is a metabolic regulator of proteostasis in the aged and Alzheimer disease brain.

bioRxiv : the preprint server for biology·2023
Same author

Dissociation between individual differences in self-reported pain intensity and underlying fMRI brain activation.

Nature communications·2022
Same journal

Reduction of secondary 3-keto bile acids by aldo-keto reductase 1C1 and 1C4.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

High-level expression of full-length human CYP2E1 in Escherichia coli: Comparison of full-length human CYP2E1 to truncated counterpart shows enhanced association with redox partners.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Construction of a curated human pharmacokinetics database for molecular fragment analysis and machine learning applications.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Finding the dispersion number (D<sub>N</sub>) of the dispersion model from perfused rat and human liver studies.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Role of organic anion transporting polypeptides in pancreatic statin disposition and islet cell function in mice.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

The regulatory potential of cytochrome P450-adrenodoxin interactions: Insights toward understanding redox partner regulation in drug metabolizing enzymes.

Drug metabolism and disposition: the biological fate of chemicals·2026
See all related articles

Researchers identified a human UDP-glucuronosyltransferase (UGT) responsible for metabolizing morphine. This enzyme, UGT2B7, is crucial for processing morphine and related opioids in the human body.

Area of Science:

  • Pharmacology
  • Biochemistry
  • Genetics

Background:

  • Opioid metabolism is critical for drug efficacy and safety.
  • UDP-glucuronosyltransferases (UGTs) play a key role in drug detoxification.
  • Previous studies lacked identification of the specific UGT isoform responsible for morphine glucuronidation.

Purpose of the Study:

  • To identify the specific human UDP-glucuronosyltransferase (UGT) isoform responsible for morphine glucuronidation.
  • To characterize the substrate specificity of the identified UGT isoform.
  • To elucidate the role of this UGT in the metabolism of clinically significant opioids.

Main Methods:

  • Isolation and sequencing of a full-length human liver cDNA.
  • Transfection of the cDNA into HK 293 cells for stable expression of the UGT isoform.

Related Experiment Videos

  • Enzymatic assays using cell homogenates and membrane preparations to assess glucuronidation activity.

    • Main Results:

    • A human UGT cDNA identical to UGT2B7 (with tyrosine at position 288) was isolated and expressed.
    • UGT2B7-expressing cells demonstrated significant glucuronidation of morphine at the 3- and 6-hydroxy positions.
    • UGT2B7 also metabolized codeine and other opioid agonists, antagonists, and partial agonists, representing the first UGT shown to act on both 3- and 6-positions of opioids.

    Conclusions:

    • UGT2B7 is identified as a major human isoform responsible for the glucuronidation of morphine.
    • This finding provides critical insight into the metabolic pathways of morphine and related opioid drugs.
    • UGT2B7's broad substrate specificity suggests its significant role in the pharmacokinetics of various opioid medications.