Biology:Deuterolysin
From HandWiki
| Deuterolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.39 | ||||||||
| CAS number | 247028-11-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Deuterolysin (EC 3.4.24.39, Penicillium roqueforti protease II, microbial neutral proteinase II, acid metalloproteinase, neutral proteinase II, Penicillium roqueforti metalloproteinase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Preferential cleavage of bonds with hydrophobic residues in P1'; also Asn3-Gln and Gly8-Ser bonds in insulin B chain
This enzyme is present in Penicillium roqueforti, P. caseicolum, Pyricularia oryzae, Aspergillus sojae and A. oryzae.
References
- ↑ "Purification and properties of neutral proteinase II from Aspergillus oryzae". Agric. Biol. Chem. 37 (12): 2703–2708. 1973. doi:10.1271/bbb1961.37.2703.
- ↑ "[The proteolytic system of Penicillium roqueforti. III. - Purification, properties and specificity of a protease inhibited by E.D.T.A]". Biochimie 56 (10): 1323–32. 1974. doi:10.1016/s0300-9084(75)80017-4. PMID 4219726.
- ↑ "Neutral proteinases I and II of Aspergillus sojae action on various substrates". Agric. Biol. Chem. 40 (4): 703–709. 1976. doi:10.1271/bbb1961.40.703.
- ↑ "Metalloproteases from Penicillium caseicolum and P. roqueforti: comparison of specificity and chemical characterization". The International Journal of Biochemistry 12 (3): 451–5. 1980. doi:10.1016/0020-711x(80)90127-5. PMID 6998789.
- ↑ "Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae". Biochemistry (Moscow) 53: 1171–1178. 1988.
External links
- Deuterolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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