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// Workers AI · dad joke modeWhat did deuterolysin say? "I'm a lysin to break bonds

From Wikipedia, the free encyclopedia
Deuterolysin
Identifiers
EC no.3.4.24.39
CAS no.247028-11-1
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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  1. Nakadai T, Nasuno S, Iguchi N (1973). "Purification and properties of neutral proteinase II from Aspergillus oryzae". Agric. Biol. Chem. 37 (12): 2703–2708. doi:10.1271/bbb1961.37.2703.
  2. Gripon JC, Hermier J (1974). "[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. 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 (4): 703–709. doi:10.1271/bbb1961.40.703.
  4. Gripon JC, Auberger B, Lenoir J (1980). "Metalloproteases from Penicillium caseicolum and P. roqueforti: comparison of specificity and chemical characterization". The International Journal of Biochemistry. 12 (3): 451–5. doi:10.1016/0020-711x(80)90127-5. PMID 6998789.
  5. Vaganova TI, Ivanova NM, Stepanov VM (1988). "Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae". Biochemistry (Moscow). 53: 1171–1178.
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