Biology:Deuterolysin

From HandWiki
Deuterolysin
Identifiers
EC number3.4.24.39
CAS number247028-11-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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, Pyricularia oryzae, Aspergillus sojae and A. oryzae.

References

  1. "Purification and properties of neutral proteinase II from Aspergillus oryzae". Agric. Biol. Chem. 37 (12): 2703–2708. 1973. doi:10.1271/bbb1961.37.2703. 
  2. "[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. 
  3. "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. 
  4. "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. 
  5. "Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae". Biochemistry (Moscow) 53: 1171–1178. 1988. 

External links