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Endopeptidases and prohormone processing.

N J Darby1, D G Smyth

  • 1National Institute for Medical Research, Mill Hill, London.

Bioscience Reports
|February 1, 1990
PubMed
Summary
This summary is machine-generated.

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Peptide hormones are made from polypeptide precursors through specific cleavage. Processing varies by tissue, suggesting enzymes recognize structure and modifications influence accessibility.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • Peptide hormones and transmitters derive from polypeptide precursors.
  • Cleavage occurs at basic residues, but processing is tissue-specific.
  • This implies complex regulation beyond simple cleavage sites.

Purpose of the Study:

  • To review recent advances in characterizing proteolytic processing enzymes.
  • To examine factors influencing restricted propeptide processing.
  • To discuss new approaches for understanding these mechanisms.

Main Methods:

  • Review of recent literature on proteolytic processing.
  • Analysis of factors affecting enzyme specificity and substrate accessibility.
  • Discussion of emerging methodologies for mechanistic studies.

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Main Results:

  • Processing of propeptides is not random and varies by tissue origin.
  • Enzyme specificity may involve recognition of peptide structure beyond basic residues.
  • Post-translational modifications can affect enzyme access to cleavage sites.

Conclusions:

  • Restricted proteolytic processing is regulated by enzyme specificity and substrate conformation.
  • Factors like glycosylation and phosphorylation play a role in accessibility.
  • Further research is needed to fully elucidate the mechanisms of propeptide processing.