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Related Experiment Videos

Relationship between lipase and esterase.

T Tsujita1, K Shirai, Y Saito

  • 1Department of Medical Biochemistry, School of Medicine, Ehime University, Japan.

Progress in Clinical and Biological Research
|January 1, 1990
PubMed
Summary
This summary is machine-generated.

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Lipase and esterase enzymes share similar catalytic sites. Introducing a hydrophobic site converts esterase into lipase, altering substrate specificity and enzyme function.

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Lipases and esterases are enzymes with distinct substrate specificities.
  • Enzyme function is often modulated by specific binding sites.

Purpose of the Study:

  • To investigate the roles of catalytic and hydrophobic recognition sites in lipase and esterase activity.
  • To explore the interconversion between lipase and esterase activities.

Main Methods:

  • Proteolytic digestion of hepatic triglyceride lipase with trypsin.
  • Enzymatic assays using water-insoluble and water-soluble ester substrates.
  • Treatment of human serum carboxylesterase with cardiolipin.

Main Results:

  • Proteolytic digestion altered hepatic triglyceride lipase activity, reducing water-insoluble ester hydrolysis while maintaining water-soluble activity.

Related Experiment Videos

  • Hepatic triglyceride lipase treated with trypsin exhibited esterase-like properties.
  • Cardiolipin enhanced triolein hydrolysis (lipase activity) in carboxylesterase and decreased tributyrin hydrolysis (esterase activity).
  • Conclusions:

    • Lipase and esterase possess similar catalytic sites.
    • The presence of a hydrophobic recognition site is crucial for converting esterase to lipase activity.