Deuterolysin
Deuterolysin | |||||||||
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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, Aspergillus sojae and A. oryzae.
References
- ↑ Nakadai, T.; Nasuno, S.; Iguchi, N. (1973). "Purification and properties of neutral proteinase II from Aspergillus oryzae". Agric. Biol. Chem. 37: 2703–2708. doi:10.1271/bbb1961.37.2703.
- ↑ Gripon, J.-C.; Hermier, J. (1974). "Le système protéolytique de Penicillium roqueforti. III. Purification, propriétés et spécificité d’une protéase inhibée par l’E.D.T.A". Biochimie. 56: 1324–1332. doi:10.1016/s0300-9084(75)80017-4. PMID 4219726.
- ↑ Sekine, H. (1976). ", Neutral proteinases I and II of Aspergillus sojae action on various substrates". Agric. Biol. Chem. 40: 703–709. doi:10.1271/bbb1961.40.703.
- ↑ Gripon, J.C.; Auberger, B.; Lenoir, J. (1980). "Metalloproteases from Penicillium caseicolum and P. roqueforti: comparison of specificity and chemical characterization". Int. J. Biochem. 12: 451–455. doi:10.1016/0020-711x(80)90127-5. PMID 6998789.
- ↑ Vaganova, T.I.; Ivanova, N.M.; Stepanov, V.M. (1988). "Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae". Biochemistry (Mosc). 53: 1171–1178.
External links
- Deuterolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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