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Deuterolysin

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Deuterolysin
Identifiers
EC no.3.4.24.39
CAS no.247028-11-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
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MetaCycmetabolic pathway
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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

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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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