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Related Experiment Videos

Structural and functional characterisation of human sulfotransferases

L A Brix1, R Nicoll, X Zhu

  • 1Department of Physiology and Pharmacology, The University of Queensland, Brisbane, Australia.

Chemico-Biological Interactions
|May 5, 1998
PubMed
Summary

Human aryl sulfotransferases HAST4 and HAST4v differ in two amino acids, affecting substrate affinity. Chimeric constructs reveal the COOH-terminal region is crucial for cofactor binding in sulfotransferases.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Human aryl sulfotransferases (HASTs) catalyze sulfonation reactions.
  • HAST4 and HAST4v exhibit distinct substrate affinities despite minor amino acid differences.

Purpose of the Study:

  • To investigate the functional impact of specific amino acid variations between HAST4 and HAST4v.
  • To identify the region responsible for differential cofactor binding affinity.

Main Methods:

  • Construction of chimeric HAST4/HAST4v proteins.
  • Enzyme kinetics analysis to determine Km for 3'-phosphoadenosine-5'-phosphosulfate (PAPS).

Main Results:

  • A chimeric construct (HAST4 with HAST4v's C-terminus) showed HAST4v-like PAPS affinity.

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  • The reverse chimeric construct (HAST4v with HAST4's C-terminus) exhibited HAST4-like PAPS affinity.

    • Conclusions:

    • The C-terminal region of human aryl sulfotransferases plays a significant role in 3'-phosphoadenosine-5'-phosphosulfate (PAPS) binding.
    • Amino acid variations in the C-terminus are critical for modulating enzyme kinetics and cofactor interaction.