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chromogenic succinyl-tripeptide-4-nitroanilide + H2O
?
Hammarsten casein + H2O
?
N-benzyloxycarbonyl-L-leucyl-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-L-leucine + 4-nitrophenol
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Phe + 4-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
?
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
N-succinyl-Ala-Ala-Val-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Val-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Pro-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Pro-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Gly-betaAla-Ala-4-nitroanilide + H2O
N-succinyl-Gly-betaAla-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
N-succinyl-Gly-Gly-Phe + 4-nitroaniline
N-succinyl-Ile-betaAla-Ala-4-nitroanilide + H2O
N-succinyl-Ile-betaAla-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ile-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ile-Val-Ala + 4-nitroaniline
N-succinyl-Leu-betaAla-Ala-4-nitroanilide + H2O
N-succinyl-Leu-betaAla-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
N-succinyl-Phe-betaAla-Ala-4-nitroanilide + H2O
N-succinyl-Phe-betaAla-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Leu-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Leu-Ala + 4-nitroaniline
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
N-succinyl-Phe-Val-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Val-Ala + 4-nitroaniline
N-succinyl-Phe-Val-Leu-4-nitroanilide + H2O
N-succinyl-Phe-Val-Leu + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Val-Phe-4-nitroanilide + H2O
N-succinyl-Phe-Val-Phe + 4-nitroaniline
-
-
-
?
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide + H2O
?
-
-
-
?
oxidized insulin chain B + H2O
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
additional information
?
-
casein + H2O
?
-
-
-
?
chromogenic succinyl-tripeptide-4-nitroanilide + H2O
?
-
-
-
?
chromogenic succinyl-tripeptide-4-nitroanilide + H2O
?
-
-
-
?
elastin-orcein + H2O
?
-
at 40°C, pH 7.5
-
-
?
elastin-orcein + H2O
?
-
at 40°C, pH 7.5
-
-
?
Hammarsten casein + H2O
?
-
at 70°C, pH 7.5-10.4
-
-
?
Hammarsten casein + H2O
?
-
at 70°C, pH 7.5-10.4
-
-
?
N-benzyloxycarbonyl-L-leucyl-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-L-leucine + 4-nitrophenol
-
-
-
?
N-benzyloxycarbonyl-L-leucyl-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-L-leucine + 4-nitrophenol
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
synthetic substrate for elastase
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
synthetic substrate for elastase
-
?
N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
synthetic substrate for subtilisin
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
N-succinyl-Gly-Gly-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
N-succinyl-Gly-Gly-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-Ile-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ile-Val-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Ile-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ile-Val-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ile-Val-Ala-4-nitroanilide + H2O
N-succinyl-Ile-Val-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Ala-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Leu-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Leu-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Leu-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Leu-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Nle-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Nle-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Val-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Val-Ala + 4-nitroaniline
-
-
-
?
N-succinyl-Phe-Val-Ala-4-nitroanilide + H2O
N-succinyl-Phe-Val-Ala + 4-nitroaniline
-
-
-
?
oxidized insulin chain B + H2O
?
-
cleavage sites are not specific
-
?
oxidized insulin chain B + H2O
?
-
at 40°C, pH 7.5
-
-
?
oxidized insulin chain B + H2O
?
-
at 40°C, pH 7.5
-
-
?
oxidized insulin chain B + H2O
?
-
cleavage sites are not specific
-
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
at 40°C, pH 7.5
-
-
?
Suc-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Phe + p-nitroaniline
-
at 40°C, pH 7.5
-
-
?
additional information
?
-
-
enzyme has 3 subsites S1, S2 and S3 in its substrate binding site. S1 site prefers alanine and phenylalanine, S2 site prefers alanine and norleucine, S3 site prefers phenylalanine and isoleucine
-
?
additional information
?
-
-
preferentially hydrolyzes the ester bond of an alanine ester, but also shows relatively strong activity toward Gly, Trp, Phe and Tyr esters
-
?
additional information
?
-
-
requires its propeptide ProA to function as an intramolecular chaperone, N-terminal IMC can inhibit aqualysin activity and form a stable complex with subtilisin BPN'
-
?
additional information
?
-
-
exhibits specificity toward ester of amino acids with small haydrophobic or aromatic residues in P1
-
-
?
additional information
?
-
-
exhibits specificity toward ester of amino acids with small haydrophobic or aromatic residues in P1
-
-
?
additional information
?
-
-
enzyme has 3 subsites S1, S2 and S3 in its substrate binding site. S1 site prefers alanine and phenylalanine, S2 site prefers alanine and norleucine, S3 site prefers phenylalanine and isoleucine
-
?
additional information
?
-
-
preferentially hydrolyzes the ester bond of an alanine ester, but also shows relatively strong activity toward Gly, Trp, Phe and Tyr esters
-
?
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1.1 - 20
N-succinyl-Ala-Ala-Ala-4-nitroanilide
0.91 - 1.7
N-succinyl-Ala-Ala-Phe-4-nitroanilide
0.49 - 3.06
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
1.6
N-succinyl-Ala-Ala-Val-4-nitroanilide
-
pH 7.4, 40°C
0.4 - 0.7
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
0.79
N-succinyl-Ala-Pro-Ala-4-nitroanilide
-
pH 7.4, 40°C
1.6 - 5.3
N-succinyl-Gly-Gly-Phe-4-nitroanilide
0.064 - 1
N-succinyl-Ile-Val-Ala-4-nitroanilide
0.04 - 44
N-succinyl-Phe-Ala-Ala-4-nitroanilide
0.087 - 71
N-succinyl-Phe-Leu-Ala-4-nitroanilide
0.036 - 730
N-succinyl-Phe-Nle-Ala-4-nitroanilide
0.039 - 1200
N-succinyl-Phe-Val-Ala-4-nitroanilide
0.41
N-succinyl-Phe-Val-Leu-4-nitroanilide
-
pH 7.4, 40°C
2.6 - 2.9
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
1.1
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, absence of DMSO
1.1
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
1.3
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.4, 40°C
2.1
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131D mutant
2.1
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202H mutant
2.3
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131K mutant
3.8
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202E mutant
7.1
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131H mutant
9.3
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, presence of DMSO
10
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202K mutant
20
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7, 50°C
0.91
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.4, 40°C
0.91
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, wild-type
1
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101V mutant
1.5
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101L mutant
1.7
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
0.49
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G131D mutant
0.69
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
wild type enzyme, 40°C, pH 7.5
0.72
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P268T mutant enzyme, 40°C, pH 7.5
0.73
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101V mutant
0.74
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P7I mutant enzyme, 40°C, pH 7.5
0.74
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D183N
0.75
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P5N mutant enzyme, 40°C, pH 7.5
0.76
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101L mutant
0.77
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D138N
0.79
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P240N mutant enzyme, 40°C, pH 7.5
0.79
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
wild type enzyme, 40°C, pH 7.5
0.79
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, wild-type enzyme
0.8
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant S277D
0.82
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant G61D
0.91
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant E237Q
0.93
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant G262D
0.98
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D17N
0.99
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D58N
1.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
40°C pH 7.5, N219T mutant
1.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, S202E mutant
1.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D212N
1.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 40°C
1.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C
1.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, wild-type
1.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
40°C pH 7.5, wild-type
1.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
1.37
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
C99S mutant enzyme, 40°C, pH 7.5
1.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, S202K mutant
1.8
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, S202H mutant
1.9
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G131H mutant
2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G131K mutant
2.17
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
C194S P7I mutant enzyme, 40°C, pH 7.5
2.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
40°C pH 7.5, N219S mutant
3.06
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
C99S/C194S mutant enzyme, 40°C, pH 7.5
0.4
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
-
40°C pH 7.5, N219T mutant
0.5
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
-
40°C pH 7.5, N219S mutant
0.7
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
-
40°C pH 7.5, wild-type
1.6
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.4, 40°C
1.6
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, wild-type
3.4
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101V mutant
4.2
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
5.3
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101L mutant
0.064
N-succinyl-Ile-Val-Ala-4-nitroanilide
-
pH 7.4, 40°C
0.064
N-succinyl-Ile-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, absence of DMSO
1
N-succinyl-Ile-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, presence of DMSO
0.04
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.4, 40°C
0.04
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, absence of DMSO
0.044
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
0.15
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202K mutant
0.24
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202H mutant
0.34
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202E mutant
0.51
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131K mutant
0.52
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131H mutant
1
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131D mutant
2.2
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, presence of DMSO
44
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
0.087
N-succinyl-Phe-Leu-Ala-4-nitroanilide
-
pH 7.4, 40°C
71
N-succinyl-Phe-Leu-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
0.036
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.4, 40°C
0.036
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.5, 40°C
0.037
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
40°C, pH 7.5, precursor protein
0.05
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
40°C, pH 7.5, mature protein
36
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
730
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
0.039
N-succinyl-Phe-Val-Ala-4-nitroanilide
-
pH 7.4, 40°C
39
N-succinyl-Phe-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
1200
N-succinyl-Phe-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
2.6
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
-
40°C pH 7.5, N219T mutant
2.7
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
-
40°C pH 7.5, N219S mutant
2.9
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
-
40°C pH 7.5, wild-type
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.5 - 8.5
N-succinyl-Ala-Ala-Ala-4-nitroanilide
0.009 - 2.5
N-succinyl-Ala-Ala-Phe-4-nitroanilide
0.014 - 296
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.047
N-succinyl-Ala-Ala-Val-4-nitroanilide
-
pH 7.4, 40°C
9 - 24
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
0.48
N-succinyl-Ala-Pro-Ala-4-nitroanilide
-
pH 7.4, 40°C
0.024 - 0.25
N-succinyl-Gly-Gly-Phe-4-nitroanilide
5 - 8.1
N-succinyl-Ile-Val-Ala-4-nitroanilide
0.1 - 11
N-succinyl-Phe-Ala-Ala-4-nitroanilide
3.3 - 3.6
N-succinyl-Phe-Leu-Ala-4-nitroanilide
0.18 - 47400
N-succinyl-Phe-Nle-Ala-4-nitroanilide
0.18 - 4.7
N-succinyl-Phe-Val-Ala-4-nitroanilide
0.069
N-succinyl-Phe-Val-Leu-4-nitroanilide
-
pH 7.4, 40°C
5
N-succinyl-Phe-Val-Phe-4-nitroanilide
-
pH 7.4, 40°C
17 - 42
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
0.5
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202E mutant
1.1
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, presence of DMSO
1.2
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
1.3
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, absence of DMSO
1.4
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.4, 40°C
1.6
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202H mutant
2.4
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131D mutant
2.6
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7, 50°C
5.4
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131K mutant
7.3
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131H mutant
8.5
N-succinyl-Ala-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202K mutant
0.009
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101L mutant
0.091
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101V mutant
0.22
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
2.5
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.4, 40°C
2.5
N-succinyl-Ala-Ala-Phe-4-nitroanilide
-
pH 7.5, 40°C, wild-type
0.014
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101L mutant
0.24
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
wild type enzyme, 40°C, pH 7.5
0.88
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
0.9
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101V mutant
2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P5N mutant enzyme, 40°C, pH 7.5
3.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
C99S/C194S mutant enzyme, 40°C, pH 7.5
3.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.4, 40°C
3.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C
6.08
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
6.4
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
C194S mutant enzyme, 40°C, pH 7.5
7.9
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G131D mutant
8.9
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G131H mutant
9
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, G131K mutant
25
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, S202E mutant
33
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, wild-type
47.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant G61D
53
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D183N
54
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, S202H mutant
59.5
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D138N
61.3
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant G262D
62
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
C99S mutant enzyme, 40°C, pH 7.5
66
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
40°C pH 7.5, N219T mutant
66.5
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P7I mutant enzyme, 40°C, pH 7.5
68.5
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D58N
72.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P5N mutant enzyme, 40°C, pH 7.5
73.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant S277D
75.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D212N
80.4
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
wild type enzyme, 40°C, pH 7.5
84
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
40°C pH 7.5, wild-type
85.2
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P240N mutant enzyme, 40°C, pH 7.5
88.7
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
P268T mutant enzyme, 40°C, pH 7.5
91.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
wild type enzyme, 40°C, pH 7.5
91.6
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, wild-type enzyme
96.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant E237Q
98.1
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
wild type enzyme, 40°C, pH 7.5
110
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
pH 7.5, 40°C, mutant D17N
144
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
pH 7.5, 40°C, S202K mutant
296
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
40°C pH 7.5, N219S mutant
9
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
-
40°C pH 7.5, N219T mutant
18
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
-
40°C pH 7.5, wild-type
24
N-succinyl-Ala-Ala-Val-Ala-4-nitroanilide
-
40°C pH 7.5, N219S mutant
0.024
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101L mutant
0.15
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.4, 40°C
0.15
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, wild-type
0.17
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
0.25
N-succinyl-Gly-Gly-Phe-4-nitroanilide
-
pH 7.5, 40°C, G101V mutant
5
N-succinyl-Ile-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, absence of DMSO
8.1
N-succinyl-Ile-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, presence of DMSO
0.1
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.4, 40°C
0.1
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, absence of DMSO
0.11
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202E mutant
0.11
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202H mutant
0.18
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, presence of DMSO
1.1
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131H mutant
1.5
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, G131K mutant
2.9
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, S202K mutant
11
N-succinyl-Phe-Ala-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
3.3
N-succinyl-Phe-Leu-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
3.6
N-succinyl-Phe-Leu-Ala-4-nitroanilide
-
pH 7.4, 40°C
0.18
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
8.8
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.4, 40°C
8.8
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.5, 40°C
8.8
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
20400
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
40°C, pH 7.5, precursor protein
47400
N-succinyl-Phe-Nle-Ala-4-nitroanilide
-
40°C, pH 7.5, mature protein
0.18
N-succinyl-Phe-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, G101A mutant
4.7
N-succinyl-Phe-Val-Ala-4-nitroanilide
-
pH 7.5, 40°C, wild-type
17
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
-
40°C pH 7.5, N219T mutant
26
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
-
40°C pH 7.5, wild-type
42
N-tert-butyloxycarbonyl-Val-Leu-Gly-Arg-4-nitroanilide
-
40°C pH 7.5, N219S mutant
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C194S
-
6% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
C5A/C8A
-
intracellular distribution similar to wild-type enzyme
C5S/C8S
-
intracellular distribution similar to wild-type enzyme
C99S
-
69% of wild type activity at 40°C, almost as stable as the wild type enzyme, similar secondary structure as the wild type enzyme
C99S/C194S
-
3% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
D138N
site-sirected mutagenesis
D17N
site-sirected mutagenesis, the mutant is less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis
D183N
site-sirected mutagenesis, the disruption of a salt bridge common to proteinase K subfamily enzymes in the D183N mutant results in a significant reduction in thermal stability, and a massive change in the content of the secondary structure compared to the wild-type enzyme
D212N
site-sirected mutagenesis, thermal stability of D212N is similar to that of the wild-type enzyme at 70°C, but it is inactivated rapidly at 80°C, the mutant is more prone to unfolding at 80°C than the wild-type enzyme
D58N
site-sirected mutagenesis
E237Q
site-sirected mutagenesis, the mutant is less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis. Disruption of a salt bridge in E237Q results in a rapid decrease of activity during incubation at 70°C and 80°C
G101A
-
catalytic efficiencies for bulky amino acid residues in P2 site such as valine and lucine drastically decreased
G101L
-
reduced catalytic efficiencies for any substrate
G101V
-
catalytic efficiency toward glycine was retained
G131D
-
reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
G131H
-
reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
G131K
-
reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
G262D
site-sirected mutagenesis
G61D
site-sirected mutagenesis
N219S
-
increased catalytic activity
N219T
-
slightly decreased catalytic activity
P240N
-
no effect on the specific activity, almost no effect on the thermostability of the protein
P268T
-
no effect on the specific activity, mutation reduces the thermostability of the protein
P5N
-
no effect on the specific activity, mutation reduces the thermostability of the protein
P7I
-
no effect on the specific activity mutation strongly reduces the thermostability of the protein
S102E
-
reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
S102H
-
reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
S102H/G131H
-
enzyme can be inhibited by metal ions
S102K
-
reduced efficiency for N-succinyl-Phe-Ala-Ala-4-nitroanilide, raised kcat for N-succinyl-Ala-Ala-Ala-4-nitroanilide
S277D
site-sirected mutagenesis
C194S
-
6% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
-
C5A/C8A
-
intracellular distribution similar to wild-type enzyme
-
C5S/C8S
-
intracellular distribution similar to wild-type enzyme
-
C99S
-
69% of wild type activity at 40°C, almost as stable as the wild type enzyme, similar secondary structure as the wild type enzyme
-
C99S/C194S
-
3% of wild type activity at 40°C, less thermostable than the wild type enzyme, similar secondary structure as the wild type enzyme
-
D138N
-
site-sirected mutagenesis
-
D17N
-
site-sirected mutagenesis, the mutant is less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis
-
D183N
-
site-sirected mutagenesis, the disruption of a salt bridge common to proteinase K subfamily enzymes in the D183N mutant results in a significant reduction in thermal stability, and a massive change in the content of the secondary structure compared to the wild-type enzyme
-
D58N
-
site-sirected mutagenesis
-
P240N
-
no effect on the specific activity, almost no effect on the thermostability of the protein
-
P268T
-
no effect on the specific activity, mutation reduces the thermostability of the protein
-
P5N
-
no effect on the specific activity, mutation reduces the thermostability of the protein
-
P7I
-
no effect on the specific activity mutation strongly reduces the thermostability of the protein
-
additional information
-
when the structure of VPR, a subtilisin-like protease isolated from Vibrio-strain PA44, is compared to a homology model of the more closely related aqualysin I a putative salt bridge between Asp17 and Arg259 is identified in the thermophilic protein, but not in VPR which has Asn15 and Lys257 in corresponding sites
additional information
amino acid residues participating in salt bridges common to proteinase K subfamily members and intrinsic to the enzyme are replaced to disrupt the bridges one at a time
additional information
-
amino acid residues participating in salt bridges common to proteinase K subfamily members and intrinsic to the enzyme are replaced to disrupt the bridges one at a time
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
75.7
-
transition temperature of the P7I mutant enzyme
83.5
-
transition temperature of the P5N mutant enzyme
86.5
-
transition temperature of the P268T mutant enzyme
86.7
-
transition temperature of the C194S mutant
86.9
-
transition temperature of the C99S/C194S mutant
89.8
-
transition temperature of the C99S mutant
91.8
-
transition temperature of the P240N mutant enzyme
94
-
transition temperature of the wild type enzyme
95
-
presence of Ca2+, 25% activity after 30 min
additional information
significance of salt bridges in the thermal stability of the enzyme, overview
100
-
10 min incubation, wild type retains 40% of activity, complete loss of activity of the C194S and C99S/C194S mutant enzymes
100
-
half of the activity of the P268T mutant is lost within a few min
100
-
wild type and P240N mutant retain 50% of activity after 5 min incubation at 100°C
70
-
80% activity after 30 min
70
-
P7I mutant is less thermostable than the wild type enzyme and other mutants in the study, complete loss of activity upon 2 h incubation at 70°C, half life: 60 min
70
-
wild type and P240N mutant retain 60% of activity after 2 h incubation at 60°C
70 - 80
-
P268T mutant almost as stable as the wild type enzyme
70 - 80
0-120 min, pH 6.0, different stabilities of wild-type and mutant enzymes at 70-80°C, inactivations, overview. The inactivation mechanism of enzyme mutant D212N at 80°C may be different from that of enzyme mutants D17N and E237Q at 70°C
80
-
rapid inactivation in absence of Ca2+
80
-
Sr2+ and Ca2+ stabilize the enzyme to heat treatment
80
-
stable in presence of 1 mM Ca2+, after gel filtration to remove free Ca2+ the enzyme still binds Ca2+ but is no longer stable, La3+, Sr2+, Nd3+ and Tb3+ stabilize the enzyme
80
-
P5N mutant much more thermolabile than the wild type enzyme, half life at 80°C: 25 min
80
-
P7I mutant is less thermostable than the wild type enzyme and other mutants in the study, half life: 10 min
90
-
half-life of wild-type and N219S mutant: 120 min, half-life of N219T mutant: 60 min in presence of Ca2+
90
-
presence of Ca2+, 40% activity after 30 min
90
-
half life of P268T mutant: 30 min
90
-
half life of wild type enzyme: 45 min, half life of C194S and C99S/C194S mutant enzymes: 10 min
90
-
P5N mutant much more thermolabile than the wild type enzyme, half life at 80°C: 15 min
90
-
wild type and P240N mutant retain 50% of activity after 45 min incubation at 90°C
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Green, P.R.; Oliver, J.D.; Strickland, L.C.; Toerner, D.R.; Matsuzawa, H.; Ohta, T.
Purification, crystallization and preliminary X-ray investigation of aqualysin I, a heat-stable serine protease
Acta Crystallogr. Sect. D
D49
349-352
1993
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Kim, D.W.; Lin, S.J.; Morita, S.; Terada, I.; Matsuzawa, H.
A carboxy-terminal pro-sequence of aqualysin I prevents proper folding of the protease domain on its secretion by Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
231
535-539
1997
Thermus aquaticus
brenda
Kim, D.W.; Matsuzawa, H.
Requirement for the COOH-terminal pro-sequence in the translocation of aqualysin I across the cytoplasmic membrane in Escherichia coli
Biochem. Biophys. Res. Commun.
277
216-220
2000
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Tanaka, T.; Matsuzawa, H.; Ohta, T.
Engineering of S2 site of aqualysin I; alteration of P2 specificity by excluding P2 side chain
Biochemistry
37
17402-17407
1998
Thermus aquaticus
brenda
Lin, S.J.; Yoshimura, E.; Sakai, H.; Wakagi, T.; Matsuzawa, H.
Weakly bound calcium ions involved in the thermostability of aqualysin I, a heat-stable subtilisin-type protease of Thermus aquaticus YT-1
Biochim. Biophys. Acta
1433
132-138
1999
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Lin, S.J.; Kim, D.W.; Ryugo, Y.; Wakagi, T.; Matsuzawa, H.
Increase of the protease activity of aqualysin I, a thermostable serine protease, by replacing Asn219 near the catalytic residue Ser222
Biosci. Biotechnol. Biochem.
61
718-719
1997
Thermus aquaticus
brenda
Tanaka, T.; Matsuzawa, H.; Ohta, T.
Stability of thermostable enzyme, aqualysin I; a subtilisin-type serine protease from Thermus aquaticus YT-1
Biosci. Biotechnol. Biochem.
62
1806-1808
1998
Thermus aquaticus
brenda
Tanaka, T.; Matsuzawa, H.; Kojima, S.; Kumagai, I.; Miura, K.; Ohta, T.
P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor
Biosci. Biotechnol. Biochem.
62
2035-2038
1998
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Tanaka, T.; Matsuzawa, H.; Ohta, T.
Substrate specificity of aqualysin I, a bacterial thermophilic alkaline serine protease from Thermus aquaticus YT-1: comparison with proteinase K, subtilisin BPN' and subtilisin Carlsberg
Biosci. Biotechnol. Biochem.
62
2161-2165
1998
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Tanaka, T.; Matsuzawa, H.; Ohta, T.
Substrate specificity of aqualysin I altered by an organic solvent, DMSO
Biosci. Biotechnol. Biochem.
63
446-448
1999
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Tanaka, T.; Kikuchi, Y.; Matsuzawa, H.; Ohta, T.
Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, Ser102 and Gly131
Biosci. Biotechnol. Biochem.
64
2008-2011
2000
Thermus aquaticus
brenda
Matsuzawa, H.; Tokugawa, K.; Hamaoki, M.; Mizoguchi, M.; Taguchi, H.; Terada, I.; Kwon, S.T.; Ohta, T.
Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1
Eur. J. Biochem.
171
441-447
1988
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Lee, Y.C.; Koike, H.; Taguchi, H.; Ohta, T.; Matsuzawa, H.
Requirement of a COOH-terminal pro-sequence for the extracellular secretion of aqualysin I (a thermophilic subtilisin-type protease) in Thermus thermophilus
FEMS Microbiol. Lett.
120
69-74
1994
Thermus thermophilus
brenda
Kwon, S.T.; Matsuzawa, H.; Ohta, T.
Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1
J. Biochem.
104
557-559
1988
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Tanaka, T.; Matsuzawa, H.; Ohta, T.
Identification and designing of the S3 site of aqualysin I, a thermophilic subtilisin-related serine protease
J. Biochem.
125
1016-1021
1999
Thermus aquaticus
brenda
Marie-Claire, C.; Yabuta, Y.; Suefuji, K.; Matsuzawa, H.; Shinde, U.
Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide
J. Mol. Biol.
305
151-165
2001
Thermus aquaticus
brenda
Kurosaka, K.; Ohta, T.; Matsuzawa, H.
A 38 kDa precursor protein of aqualysin I (a thermophilic subtilisin-type protease) with a C-terminal extended sequence: its purification and in vitro processing
Mol. Microbiol.
20
385-389
1996
Thermus aquaticus
brenda
Matsuzawa, H.
Aqualysin I
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press
2
1799-1800
2004
Thermus aquaticus, Thermus aquaticus YT-1
-
brenda
Sakaguchi, M.; Matsuzaki, M.; Niimiya, K.; Seino, J.; Sugahara, Y.; Kawakita, M.
Role of proline residues in conferring thermostability on aqualysin I
J. Biochem.
141
213-220
2007
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Sakaguchi, M.; Takezawa, M.; Nakazawa, R.; Nozawa, K.; Kusakawa, T.; Nagasawa, T.; Sugahara, Y.; Kawakita, M.
Role of disulfide bonds in a thermophilic serine protease aqualysin I from Thermus aquaticus YT-1
J. Biochem.
143
625-632
2008
Thermus aquaticus, Thermus aquaticus YT-1
brenda
Sigurdardottir, A.G.; Arnorsdottir, J.; Thorbjarnardottir, S.H.; Eggertsson, G.; Suhre, K.; Kristjansson, M.M.
Characteristics of mutants designed to incorporate a new ion pair into the structure of a cold adapted subtilisin-like serine proteinase
Biochim. Biophys. Acta
1794
512-518
2009
Thermus aquaticus
brenda
Sakaguchi, M.; Niimiya, K.; Takezawa, M.; Toki, T.; Sugahara, Y.; Kawakita, M.
Construction of an expression system for aqualysin I in Escherichia coli that gives a markedly improved yield of the enzyme protein
Biosci. Biotechnol. Biochem.
72
2012-2018
2008
Thermus aquaticus
brenda
Sakaguchi, M.; Osaku, K.; Maejima, S.; Ohno, N.; Sugahara, Y.; Oyama, F.; Kawakita, M.
Highly conserved salt bridge stabilizes a proteinase K subfamily enzyme, Aqualysin I, from Thermus aquaticus YT-1
AMB Express
4
59
2014
Thermus aquaticus (P08594), Thermus aquaticus YT-1 (P08594), Thermus aquaticus YT-1
brenda
Verbauwhede, A.E.; Lambrecht, M.A.; Fierens, E.; Hermans, S.; Shegay, O.; Brijs, K.; Delcour, J.A.
Thermo-reversible inhibition makes aqualysin 1 from Thermus aquaticus a potent tool for studying the contribution of the wheat gluten network to the crumb texture of fresh bread
Food Chem.
264
118-125
2018
Thermus aquaticus
brenda
Verbauwhede, A.; Lambrecht, M.; Fierens, E.; Shegay, O.; Brijs, K.; Delcour, J.
Impact of aqualysin 1 peptidase from Thermus aquaticus on molecular scale changes in the wheat gluten network during bread baking
Food Chem.
295
599-606
2019
Thermus aquaticus
brenda