Deuterolysin

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

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

  1. 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.
  2. Gripon, J.-C.; Hermier, J. (1974). "Le système protéolytique de Penicillium roqueforti. III. Purification, propriétés et spécificité dune protéase inhibée par lE.D.T.A". Biochimie. 56: 1324–1332. doi:10.1016/s0300-9084(75)80017-4. PMID 4219726.
  3. 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.
  4. 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.
  5. 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

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