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Aminopeptidase B (EC 3.4.11.6).

T Foulon1, S Cadel, P Cohen

  • 1Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, Université Pierre et Marie Curie, Paris, France. foulon@ccr.jussieu.fr

The International Journal of Biochemistry & Cell Biology
|September 1, 1999
PubMed
Summary
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Aminopeptidase B, a zinc-dependent enzyme, cleaves specific amino acids from peptides and hydrolyzes leukotriene A4. It plays a role in precursor processing in various tissues and cellular locations.

Area of Science:

  • Biochemistry
  • Enzymology
  • Cell Biology

Background:

  • Aminopeptidase B (EC 3.4.11.6) is a zinc-dependent exopeptidase.
  • It removes arginine and lysine residues from peptide N-termini.
  • Structurally related to leukotriene A4 hydrolase.

Purpose of the Study:

  • To investigate the enzymatic activity and substrate specificity of Aminopeptidase B.
  • To explore the structural relationship between Aminopeptidase B and leukotriene A4 hydrolase.
  • To elucidate the potential role of Aminopeptidase B in cellular precursor processing.

Main Methods:

  • Analysis of primary structure.
  • Enzyme activity assays with various peptide substrates.
  • Hydrolysis assay with leukotriene A4.

Related Experiment Videos

  • Tissue distribution analysis.

    • Main Results:

    • Aminopeptidase B selectively cleaves Arg/Lys from peptide substrates like enkephalins and somatostatin.
    • Demonstrated capacity of Aminopeptidase B to hydrolyze leukotriene A4.
    • Enzyme is widely distributed and found on the plasma membrane in PC12 cells.

    Conclusions:

    • Aminopeptidase B is a bi-functional enzyme with roles in peptide processing and leukotriene metabolism.
    • Its presence in various tissues and cellular compartments suggests a significant physiological function.
    • Likely involved in final stages of precursor processing within the secretory pathway and/or at the plasma membrane.