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(4-Nitro)Phe-Nle-Ala-Leu methyl ester + H2O
Nle-Ala-Leu methyl ester + (4-nitro)Phe
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-
-
?
Ac-(Ala)m-Lys-(NO2)Phe-(Ala)n amide + H2O
?
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-
-
-
?
Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
Ac-(Ala)n-Lys + Nph-(Ala)m-amide
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-
-
?
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide + H2O
?
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-
-
-
?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala-Ala amide + H2O
Ac-Ala-Ala-Lys + (4-nitro)Phe-Ala-Ala-Ala amide
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-
-
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?
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
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?
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
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?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
Ac-Ala-Ala-Lys-(p-NO2)Phe-Ala-Ala-NH2 + H2O
?
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-
?
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
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-
?
Ac-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
Ac-Ala-Lys-Ala-(NO2)Phe-amide + H2O
?
-
-
-
-
?
Ac-Gly-Lys-(4-nitro)Phe-Ala-Ala amide + H2O
Ac-Gly-Lys + (4-nitro)Phe-Ala-Ala amide
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-
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?
Ac-Lys 4-nitrophenyl amide + H2O
?
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?
Ac-Lys-(NO2)Phe- Ala-amide + H2O
?
Ac-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
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-
-
?
Ac-Lys-(NO2)Phe-amide + H2O
?
Ac-Val-Lys-(4-nitro)Phe-Ala amide + H2O
Ac-Val-Lys + (4-nitro)Phe-Ala amide
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?
Ac-Xaa-Lys-(NO2)Phe-Ala-Ala amide + H2O
?
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?
B-chain of S-sulfo-insulin + H2O
?
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?
Bovine serum albumin + H2O
?
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cleaves 15% of the peptide bonds
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?
bovine trypsinogen + H2O
?
-
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-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHLVEALYLVCG + ERGFFYTPKA
i.e. insulin B chain, cleavage site specificity
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-
?
H-Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester + H2O
Nle-Ala-Leu methyl ester + Leu-Ser-(4-nitro)Phe
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-
-
?
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester + H2O
?
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-
-
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?
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Thr-Glu-Phe + (4-nitro)Phe-Arg-Leu
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-
-
?
trypsin inhibitor + H2O
trypsin inhibitor fragments
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substrate from Cucurbita maxima, specific cleavage of Leu7-Met8 bond at pH 3.3
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?
trypsinogen + H2O
trypsin + propeptide Val(Asn)4-Lys-OH
substrate from Bos taurus, rapid activation
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-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
additional information
?
-
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
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-
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-
?
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
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?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
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?
Ac-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
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?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Lys-(NO2)Phe- Ala-amide + H2O
?
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?
Ac-Lys-(NO2)Phe- Ala-amide + H2O
?
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?
Ac-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Lys-(NO2)Phe-amide + H2O
?
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?
Ac-Lys-(NO2)Phe-amide + H2O
?
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?
azocasein + H2O
?
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?
azocasein + H2O
?
Penicillium candidum
-
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?
azocasein + H2O
?
Penicillium candidum PCA 1/TT031
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?
Egg albumin + H2O
?
Penicillium duponti
-
best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
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?
Egg albumin + H2O
?
Penicillium duponti K 1014
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best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
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?
Hemoglobin + H2O
?
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?
Hemoglobin + H2O
?
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?
Hemoglobin + H2O
?
Penicillium duponti
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best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
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?
Hemoglobin + H2O
?
Penicillium duponti K 1014
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best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
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?
Milk casein + H2O
?
Penicillium duponti
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?
Milk casein + H2O
?
Penicillium duponti K 1014
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?
Trypsinogen + H2O
?
Penicillium duponti
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?
Trypsinogen + H2O
?
Penicillium duponti K 1014
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?
Trypsinogen + H2O
?
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?
Trypsinogen + H2O
?
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bovine, activation by cleavage of Lys6-Ile7
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-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
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rapid activation
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?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
Penicillium duponti
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rapid activation
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?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
Penicillium duponti K1014
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rapid activation
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?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
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rapid activation
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?
wheat flour + H2O
?
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?
wheat flour + H2O
?
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?
additional information
?
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broad protein substrate specificity
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?
additional information
?
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Penicillium duponti
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broad protein substrate specificity
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?
additional information
?
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Penicillium duponti K1014
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broad protein substrate specificity
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?
additional information
?
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milk clotting activity
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?
additional information
?
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acts on some small substrates with two hydrophobic amino acids at the N-terminus and a free amino group, in addition to removing the N-terminal amino acid hydrolytically a trans-peptidation reaction occurs: Leu-Leu is formed from Leu-Tyr-Leu, Phe-Phe from Phe-Tyr-Thr-Pro-Lys-Ala and Met-Met from Met-Leu-Gly
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?
additional information
?
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transpeptidation reaction of both the amino acid and the acyl transfer type
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?
additional information
?
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transpeptidation reaction of both the amino acid and the acyl transfer type
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?
additional information
?
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broad protein substrate specificity with preference for hydrophobic residues at positions P1 and P1', especially for Lys in P1 because the epsilon-amino group forms an ionic bond with the side-chain carboxylate of Asp77, substrate specificity involves the side chain of the P3 residue, mechanism, detailed overview
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-
?
additional information
?
-
broad protein substrate specificity with preference for hydrophobic residues at positions P1 and P1', especially for Lys in P1 because the epsilon-amino group forms an ionic bond with the side-chain carboxylate of Asp77, substrate specificity involves the side chain of the P3 residue, mechanism, detailed overview
-
-
?
additional information
?
-
broad protein substrate specificity with preference for hydrophobic residues at positions P1 and P1', especially for Lys in P1 because the epsilon-amino group forms an ionic bond with the side-chain carboxylate of Asp77, substrate specificity involves the side chain of the P3 residue, mechanism, detailed overview
-
-
?
additional information
?
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substrate binding specificity, cleavage site specificity, overview
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?
additional information
?
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substrate binding specificity, cleavage site specificity, overview
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?
additional information
?
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substrate binding specificity, cleavage site specificity, overview
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?
additional information
?
-
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broad protein substrate specificity
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?