Magnolysin
Magnolysin (EC 3.4.24.62, bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin, pro-oxytocin/neurophysin convertase, prooxyphysin proteinase, pro-oxytocin convertase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-Arg-Ala-Val-.
This endopeptidase is present in bovine pituitary neurosecretory granules.
References
- ↑ Clamagirand, C., Creminon, C., Fahy, C., Boussetta, H. and Cohen, P. (1987). "Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytosin/neurophysin peptides at the basic amino acid doublet". Biochemistry 26: 6018–6023. doi:10.1021/bi00393a011. PMID 2825769.
- ↑ Créminon, C., Rholam, M., Boussetta, H., Marrakchi, N. and Cohen, P. (1988). "Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme". J. Chromatogt. 440: 439–448. doi:10.1016/s0021-9673(00)94547-3. PMID 3042797.
- ↑ Brakch, N., Boussetta, H., Rholam, M. and 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: 15912–15916. PMID 2674120.
- ↑ Plevrakis, I, Créminon, C., Clamagirand, C., Brakch, N., Rholam, M. and Cohen, P. (1989). "Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor". Biochemistry 28: 2705–2710. doi:10.1021/bi00432a051. PMID 2659078.
- ↑ Guillou, M.D., Camier, M. and Clamagirand, C. (1994). "Evidence for the presence of pro-oxytocin/neurophysin converting enzyme in the human ovary". J. Endocrinol. 142: 345–352. doi:10.1677/joe.0.1420345. PMID 7931007.
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