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Structure-function studies of human aromatase

S Chen1, D Zhou, K M Swiderek

  • 1Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, CA 91010.

The Journal of Steroid Biochemistry and Molecular Biology
|March 1, 1993
PubMed
Summary
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Site-directed mutagenesis reveals that amino acids Gln-298 to Val-313 are crucial for human aromatase active site function. These findings advance understanding of aromatase structure-function relationships.

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Human aromatase is a key enzyme in estrogen biosynthesis.
  • Understanding its active site is crucial for drug development.

Purpose of the Study:

  • To elucidate the structure-function relationship of human aromatase.
  • To identify critical regions within the aromatase active site.

Main Methods:

  • Site-directed mutagenesis was used to create eight aromatase mutants.
  • Mutants were expressed in a mammalian cell stable-expression system.
  • Catalytic properties of selected mutants were analyzed.
  • HPLC-linked electrospray mass spectrometry was employed for enzyme characterization.

Main Results:

  • The region Gln-298 to Val-313, corresponding to the distal helix of cytochrome P-450cam, was identified as important.

Related Experiment Videos

  • Mutations in this region significantly impacted aromatase activity.
  • Mass spectral analysis indicated that aromatase is glycosylated.

    • Conclusions:

    • The Gln-298 to Val-313 region is vital for the active site of human aromatase.
    • Site-directed mutagenesis is a powerful tool for probing enzyme active sites.
    • Further characterization of enzyme glycosylation may be warranted.