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Aminopeptidases: structure and function

A Taylor1

  • 1U.S. Department of Agriculture Human Nutrition Research Center on Aging, Tufts University Laboratory for Nutrition and Vision Research, Boston, Massachusetts 02111.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|February 1, 1993
PubMed
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Aminopeptidases are essential enzymes that remove amino acids from proteins. Structural and sequence studies reveal conserved features in their active sites, particularly metal ion binding sites, across diverse species.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Aminopeptidases are enzymes catalyzing amino acid removal from peptide termini.
  • They are ubiquitous in nature, found in various cellular locations and performing vital functions.
  • Many are zinc metalloenzymes inhibited by bestatin, with diverse quaternary structures.

Purpose of the Study:

  • To review the structural and functional characteristics of aminopeptidases.
  • To highlight conserved features in aminopeptidase structure and catalytic mechanisms.
  • To discuss sequence homologies and their implications for enzyme function.

Main Methods:

  • Analysis of available cDNA sequences for aminopeptidase genes.
  • Review of crystallographic and electron microscopy data for enzyme structures.

Related Experiment Videos

  • Examination of NMR and photoaffinity labeling studies.

    • Main Results:

    • Bovine lens leucine aminopeptidase exhibits a bilobal protomer structure with an active site in the larger lobe.
    • Bestatin and substrates bind within the active site, with Zn2+ crucial for substrate binding in most aminopeptidases.
    • No acyl-enzyme intermediate was observed during hydrolysis.
    • Sequence homologies exist between bacterial and mammalian aminopeptidases, especially in catalytic and metal-binding regions.

    Conclusions:

    • Aminopeptidase structure and function show conserved elements across evolution.
    • Understanding these conserved features aids in elucidating enzyme mechanisms and designing inhibitors.
    • Further research into sequence-structure-function relationships is warranted.