The Enzyme Database

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EC 3.4.24.39     
Accepted name: deuterolysin
Reaction: Preferential cleavage of bonds with hydrophobic residues in P1&prime
also Asn3┼Gln and Gly8┼Ser bonds in insulin B chain
Other name(s): Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase
Comments: Proteolytic activity found in Penicillium roqueforti [4], P. caseicolum [4], Aspergillus sojae [3] and A. oryzae [1,5]. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 247028-11-1
References:
1.  Nakadai, T., Nasuno, S. and Iguchi, N. Purification and properties of neutral proteinase II from Aspergillus oryzae. Agric. Biol. Chem. 37 (1973) 2703–2708.
2.  Gripon, J.-C. and Hermier, J. Le système protéolytique de Penicillium roqueforti. III. Purification, propriétés et spécificité d’une protéase inhibée par l’E.D.T.A. Biochimie 56 (1974) 1324–1332. [PMID: 4219726]
3.  Sekine, H. , Neutral proteinases I and II of Aspergillus sojae action on various substrates. Agric. Biol. Chem. 40 (1976) 703–709.
4.  Gripon, J.C., Auberger, B. and Lenoir, J. Metalloproteases from Penicillium caseicolum and P. roqueforti: comparision of specificity and chemical characterization. Int. J. Biochem. 12 (1980) 451–455. [PMID: 6998789]
5.  Vaganova, T.I., Ivanova, N.M. and Stepanov, V.M. Isolation and properties of the "acid" metalloproteinase from Aspergillus oryzae. Biochemistry (Mosc) 53 (1988) 1171–1178.
[EC 3.4.24.39 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.39]
 
 


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