The Enzyme Database

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Accepted name: magnolysin
Reaction: Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-Arg┼Ala-Val-. The specificity further depends on the organization of a β-turn-α-helix of nine or more residues containing the paired basic amino acids near the centre [3]
Other name(s): bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase
Comments: An endopeptidase of 58 kDa known from bovine pituitary neurosecretory granules and bovine and human corpus luteum [4,5]. Inhibited by EDTA [1]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 162875-09-4
1.  Clamagirand, C., Creminon, C., Fahy, C., Boussetta, H. and Cohen, P. Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytosin/neurophysin peptides at the basic amino acid doublet. Biochemistry 26 (1987) 6018–6023. [PMID: 2825769]
2.  Créminon, C., Rholam, M., Boussetta, H., Marrakchi, N. and Cohen, P. Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme. J. Chromatogt. 440 (1988) 439–448. [PMID: 3042797]
3.  Brakch, N., Boussetta, H., Rholam, M. and Cohen, P. Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model. J. Biol. Chem. 264 (1989) 15912–15916. [PMID: 2674120]
4.  Plevrakis, I, Créminon, C., Clamagirand, C., Brakch, N., Rholam, M. and Cohen, P. Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor. Biochemistry 28 (1989) 2705–2710. [PMID: 2659078]
5.  Guillou, M.D., Camier, M. and Clamagirand, C. Evidence for the presence of pro-oxytocin/neurophysin converting enzyme in the human ovary. J. Endocrinol. 142 (1994) 345–352. [PMID: 7931007]
[EC created 1995]

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