Biology:Magnolysin
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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
- ↑ "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. September 1987. doi:10.1021/bi00393a011. PMID 2825769.
- ↑ "Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme". Journal of Chromatography 440: 439–48. May 1988. doi:10.1016/s0021-9673(00)94547-3. PMID 3042797.
- ↑ "Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model". The Journal of Biological Chemistry 264 (27): 15912–6. September 1989. PMID 2674120.
- ↑ "Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor". Biochemistry 28 (6): 2705–10. March 1989. doi:10.1021/bi00432a051. PMID 2659078.
- ↑ "Evidence for the presence of pro-oxytocin/neurophysin-converting enzyme in the human ovary". The Journal of Endocrinology 142 (2): 345–52. August 1994. doi:10.1677/joe.0.1420345. PMID 7931007.
External links
- Magnolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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