Definition
An inactive peptide precursor that requires enzymatic cleavage to become biologically active.

Detailed Explanation

An inactive peptide precursor that requires enzymatic cleavage to become biologically active. Propeptides serve as safety mechanisms: they prevent potentially harmful peptides from being active before reaching their target tissue. Proinsulin (86 amino acids) is cleaved in pancreatic β-cell secretory granules to yield mature insulin (51 aa, A+B chains) and C-peptide (31 aa).

Proenkephalin yields multiple copies of Met-enkephalin and Leu-enkephalin. Pro-opiomelanocortin (POMC, 241 aa) is a polyprotein precursor that yields ACTH, β-endorphin, and α/β/γ-MSH depending on which proteases process it in different tissues. C-peptide, once thought to be biologically inert, is now used clinically to measure endogenous insulin production in diabetic patients.

Key Facts

  • An inactive peptide precursor that requires enzymatic cleavage to become biologically active.
  • Propeptides serve as safety mechanisms: they prevent potentially harmful peptides from being active before reaching their target tissue.
  • Proinsulin (86 amino acids) is cleaved in pancreatic β-cell secretory granules to yield mature insulin (51 aa, A+B chains) and C-peptide (31 aa).
  • Proenkephalin yields multiple copies of Met-enkephalin and Leu-enkephalin.
  • Pro-opiomelanocortin (POMC, 241 aa) is a polyprotein precursor that yields ACTH, β-endorphin, and α/β/γ-MSH depending on which proteases process it in different tissues.
  • C-peptide, once thought to be biologically inert, is now used clinically to measure endogenous insulin production in diabetic patients.
Related Terms Insulin Endorphin Melanocortin Signal Peptide Protease

← Back to Full Dictionary

Part of the PeptideBond.com education network

Educational Disclaimer

PeptideDefinition.com provides educational content about peptide science. Not medical advice. Consult a licensed healthcare provider for medical decisions.