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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