Parent Class:

EC-Numbers → 3 -- Hydrolases → 3.4 -- Acting on peptide bonds (peptide hydrolases) → 3.4.24 -- Metalloendopeptidases

Synonyms: bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin, pro-oxytocin/neurophysin convertase, prooxyphysin proteinase, pro-oxytocin convertase

Unification Links: BRENDA:3.4.24.62, ENZYME:3.4.24.62, IUBMB-ExplorEnz:3.4.24.62

Reaction:
protein + H₂O → 2 peptide + 2 H⁺

Summary:
This enzyme catalyzes hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-ArgAla-Val-. The specificity further depends on the organization of a -turn--helix of nine or more residues containing the paired basic amino acids near the centre [Brakch89]

An endopeptidase of 58 kDa known from bovine pituitary neurosecretory granules and bovine and human corpus luteum [Plevrakis89], [Guillou94]. Inhibited by EDTA [Clamagirand87].

Citations: [Creminon88]

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References

Brakch89: Brakch N, Boussetta H, Rholam M, Cohen P (1989). "Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model." J Biol Chem 264(27);15912-6. PMID: 2674120

Clamagirand87: Clamagirand C, Creminon C, Fahy C, Boussetta H, Cohen P (1987). "Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytocin/neurophysin peptides at the basic amino acid doublet." Biochemistry 26(19);6018-23. PMID: 2825769

Creminon88: Creminon C, Rholam M, Boussetta H, Marrakchi N, Cohen P (1988). "Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme." J Chromatogr 440;439-48. PMID: 3042797

Guillou94: Guillou MD, Camier M, Clamagirand C (1994). "Evidence for the presence of pro-oxytocin/neurophysin-converting enzyme in the human ovary." J Endocrinol 142(2);345-52. PMID: 7931007

Plevrakis89: Plevrakis I, Clamagirand C, Creminon C, Brakch N, Rholam M, Cohen P (1989). "Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor." Biochemistry 28(6);2705-10. PMID: 2659078

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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