magnolysin

{{Infobox enzyme

| Name = Magnolysin

| EC_number = 3.4.24.62

| CAS_number = 162875-09-4

| GO_code =

| image =

| width =

| caption =

}}

Magnolysin ({{EC number|3.4.24.62}}, bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin, pro-oxytocin/neurophysin convertase, prooxyphysin proteinase, pro-oxytocin convertase) is an enzyme.{{cite journal | vauthors = Clamagirand C, Creminon C, Fahy C, Boussetta H, Cohen P | title = Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytocin/neurophysin peptides at the basic amino acid doublet | journal = Biochemistry | volume = 26 | issue = 19 | pages = 6018–23 | date = September 1987 | pmid = 2825769 | doi = 10.1021/bi00393a011 }}{{cite journal | vauthors = Créminon C, Rholam M, Boussetta H, Marrakchi N, Cohen P | title = Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme | journal = Journal of Chromatography | volume = 440 | pages = 439–48 | date = May 1988 | pmid = 3042797 | doi = 10.1016/s0021-9673(00)94547-3 }}{{cite journal | vauthors = Brakch N, Boussetta H, Rholam M, Cohen P | title = Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model | journal = The Journal of Biological Chemistry | volume = 264 | issue = 27 | pages = 15912–6 | date = September 1989 | pmid = 2674120 }}{{cite journal | vauthors = Plevrakis I, Clamagirand C, Créminon C, Brakch N, Rholam M, Cohen P | title = Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor | journal = Biochemistry | volume = 28 | issue = 6 | pages = 2705–10 | date = March 1989 | pmid = 2659078 | doi = 10.1021/bi00432a051 }}{{cite journal | vauthors = Guillou MD, Camier M, Clamagirand C | title = Evidence for the presence of pro-oxytocin/neurophysin-converting enzyme in the human ovary | journal = The Journal of Endocrinology | volume = 142 | issue = 2 | pages = 345–52 | date = August 1994 | pmid = 7931007 | doi = 10.1677/joe.0.1420345 }} 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.