Comparison of the hydrolysis of the three types of natriuretic peptides by human kidney neutral endopeptidase 24.11

Biochem Mol Med. 1997 Jun;61(1):47-51. doi: 10.1006/bmme.1997.2584.


The degradation of 3 human natriuretic peptides by human kidney neutral endopeptidase 24.11 has been investigated. The studies revealed that hANP-28 and hCNP-22 are the preferred substrates, whereas hBNP-32 is not. The enzyme has been known to inactivate hANP-28 from cleavage at the Cys-Phe bond at the beginning of its ring structure. Analysis of the cleavage sites of each peptide indicated that the initial cleavage site of hCNP-22 is analogous to that of hANP-28. The Cys-Phe bond of hBNP-32 was insensitive to this enzymatic cleavage. We speculate that the stability of hBNP-32 may result from the insusceptibility of its Cys-Phe bond at the beginning of the ring structure.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Atrial Natriuretic Factor / metabolism
  • Enzyme Activation
  • Humans
  • Hydrolysis
  • Kidney / enzymology*
  • Kinetics
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Natriuretic Agents / metabolism*
  • Natriuretic Peptide, Brain*
  • Natriuretic Peptide, C-Type
  • Neprilysin / metabolism*
  • Nerve Tissue Proteins / metabolism
  • Proteins / metabolism


  • Membrane Proteins
  • Natriuretic Agents
  • Nerve Tissue Proteins
  • Proteins
  • Natriuretic Peptide, Brain
  • brain natriuretic peptide, porcine
  • Natriuretic Peptide, C-Type
  • Atrial Natriuretic Factor
  • Neprilysin