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Ursula Kettmann1, H Hanson

  • 1Physiologisch-chemisches Institut der Martin-Luther-Universität, Halle/Saale, GDR

FEBS Letters
|September 18, 1970
PubMed
Summary

Bovine lens leucine aminopeptidase is a zinc metalloenzyme. Removal of zinc results in an inactive apo-enzyme, and reactivation with zinc ions is not possible, indicating specific zinc binding.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Metalloprotein chemistry

Background:

  • Leucine aminopeptidase is a key enzyme in the bovine lens.
  • Metalloenzymes play crucial roles in various biological processes.
  • Understanding the role of metal ions in enzyme structure and function is vital.

Purpose of the Study:

  • To characterize the zinc content and binding properties of bovine lens leucine aminopeptidase.
  • To investigate the enzyme's dependence on zinc for activity.
  • To explore the binding of other divalent metal ions and the influence of pH and buffer on zinc binding.

Main Methods:

  • Radioactive labeling with 65Zn.
  • Atomic absorption spectrophotometry for zinc quantification.
  • Dialysis against o-phenanthroline to remove zinc.
  • Investigation of metal ion binding (Cd2+, Mn2+, Co2+).

Main Results:

  • Bovine lens leucine aminopeptidase contains 5.0-7.6 g-atoms of Zn per MW of 3.2 x 10(6).
  • Zinc removal via dialysis yielded an inactive apo-enzyme.
  • Reactivation of the apo-enzyme with Zn2+ was unsuccessful.
  • Manganese may bind to a different site than zinc.
  • pH and buffer ions affect zinc binding.

Conclusions:

  • Bovine lens leucine aminopeptidase is a zinc-dependent metalloenzyme.
  • The enzyme's structure and activity are critically dependent on zinc binding.
  • The apo-enzyme cannot be readily reactivated, suggesting a stable or irreversible zinc-binding site.
  • Other metal ions and environmental factors influence zinc binding and enzyme activity.

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