ENTRY EC 3.4.24.39
NAME Deuterolysin
Penicillium roqueforti protease II
Microbial neutral proteinase II
Acid metalloproteinase
CLASS Hydrolases
Acting on peptide bonds (peptidases)
Metalloendopeptidases
REACTION Preferential cleavage of bonds with hydrophobic residues in P1';
also Asn3+Gln and Gly8+Ser bonds in insulin B chain.
SUBSTRATE Protein
Peptide
H2O
PRODUCT Protein
Peptide
COFACTOR Metal
COMMENT Proteolytic activity found in Penicillium roqueforti,
P. caseicolum, Aspergillus sojae and A. oryzae. Optimum pH of 5
for digesting various proteins. Strong action on protamine and
histones. Insensitive to phosphoramidon. Mr about 20 kDa.
A distinct Aspergillus sojae endopeptidase is larger and has a
neutral pH optimum. Formerly included in EC 3.4.24.4.
MOTIF PS: PS00142 [GSTALIVN]-x(2)-H-E-[LIVMFYW]-{DEHRKP}-H-x-
[LIVMFYWGSPQ]
DBLINKS University of Geneva ENZYME DATA BANK: 3.4.24.39
WIT (What Is There) Metabolic Reconstruction: 3.4.24.39
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