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Related Experiment Videos

UDPGT cDNA expression and UDPGT1 in human liver

Y Y Sheen1, I S Owens, S S Kim

  • 1College of Pharmacy, Department of Pharmacy, Ewha Womans University, Seoul, Korea.

The Journal of Toxicological Sciences
|October 7, 1998
PubMed
Summary

The UDPGTh2 enzyme is 100 times more efficient than UDPGTh1 in metabolizing certain steroid structures. Key amino acid differences in the N-terminus of UDPGTh1 and UDPGTh2 determine substrate specificity and catalytic efficiency.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • UDP-glucuronosyltransferases (UGTs) are crucial enzymes involved in the metabolism and detoxification of various compounds.
  • Two isoforms, UDPGTh1 and UDPGTh2, exhibit distinct substrate specificities and catalytic efficiencies.

Purpose of the Study:

  • To investigate the substrate specificity and catalytic efficiency of UDPGTh1 and UDPGTh2 isoforms.
  • To identify the molecular determinants responsible for isoform-specific substrate recognition and catalytic activity.
  • To elucidate the gene structure and organization of UDPGTh1 and UDPGTh2.

Main Methods:

  • Expression of UDPGTh1 and UDPGTh2 in Cos-1 cells for metabolic assays.
  • Construction and analysis of chimeric cDNAs to map functional domains.

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  • Screening of a leukocyte DNA cosmid library and subsequent DNA sequencing and Southern blot analysis to determine gene structure.

    • Main Results:

    • Both UDPGTh1 and UDPGTh2 metabolized 3,4-catechol estrogen (4-hydroxyestrone), estriol, 17-epiestriol, and hyodeoxycholic acid (HDCA).
    • UDPGTh2 demonstrated 100-fold higher catalytic efficiency than UDPGTh1.
    • Nine amino acids between residues 385 and 469 were identified as critical for catalytic efficiency, distinct from the N-terminal domain responsible for substrate specificity.
    • The gene structure revealed a cluster of 4 common exons encoding the 3' identity region and unique upstream exons for UDPGTh1 and UDPGTh2.

    Conclusions:

    • The N-terminal region of UDPGTh1 and UDPGTh2 plays a crucial role in determining substrate specificity.
    • A distinct domain between residues 385 and 469 is essential for catalytic efficiency.
    • The UGT1A and UGT1D genes encode the unique regions of UDPGTh1 and UDPGTh2, respectively, located upstream of common exons.