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50S ribosomal protein L7/L12 + H2O
?
6-phosphogluconate dehydrogenase + H2O
?
acetyl-Lys-p-nitroaniline + H2O
acetyl-Lys + p-nitroaniline
-
-
?
acid soluble collagen + H2O
?
-
from the cartilages of brownbanded bamboo shark Chiloscyllium punctatum and blacktip shark Carcharhinus limbatus
-
-
?
ACTH + H2O
?
-
hydrolysis of the bonds: Lys11-Pro12, Lys16-Lys16, Lys16-Arg17, Lys21-Val22
-
-
?
acyl carrier protein + H2O
?
albacore tuna pepsin-solubilised collagen + H2O
?
-
-
-
-
?
amyloid beta-protein + H2O
?
B-chain of insulin + H2O
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
-
-
-
-
?
benzoyl-L-Lys-4-nitroanilide + H2O
benzoyl-L-Lys + 4-nitroaniline
benzoyl-Lys methyl ester + H2O
benzoyl-Lys + methanol
benzoyl-Lys-NH2 + H2O
benzoyl-Lys + NH3
-
-
-
-
?
benzoyl-Lys-p-nitroanilide + H2O
benzoyl-Lys + p-nitroaniline
benzoyl-Lys-p-nitroaniline + H2O
benzoyl-Lys + p-nitroaniline
-
-
?
benzoyl-Orn methyl ester + H2O
benzoyl-Orn + methanol
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
Boc-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
bovine trypsinogen + H2O
trypsin + ?
-
the enzyme activates the zymogens
-
-
?
chaperone protein DNA kinase + H2O
?
chymotrypsinogen + H2O
chymotrypsin + ?
-
-
-
-
?
Denatured hemoglobin + H2O
?
-
-
-
-
?
elongation factor G + H2O
?
elongation factor Tu + H2O
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fructose-bisphosphate aldolase class 2 + H2O
?
glyceraldehyde-3-phosphate dehydrogenase A + H2O
?
Ile-Asn-Leu-Lys-Ala-leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2
?
-
i.e. mastoparan. Cleavage sites: Ile-Asn-Leu-Lys-/-Ala-Leu-Ala-Ala-Leu-Ala-Lys-/-Lys-/-Ile-Leu-NH2
-
-
?
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2 + H2O
?
-
i.e. mastoparan, cleavage sites: Lys4-Ala5, Lys11-Lys12, Lys12-Ile13
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
Lys-p-nitroanilide + H2O
Lys + p-nitroaniline
lysine vasopressin + H2O
?
N-acetyl-L-lysine + H2O
N-acetyl-L-lysine + H2O
-
-
incorporation of O18 atom into the carboxyl group
-
?
N-benzoyl-L-Lys-p-nitroanilide + H2O
N-benzoyl-L-Lys + p-nitroaniline
N-benzoyl-L-Orn methyl ester + H2O
N-benzoyl-L-Orn + methanol
-
-
-
-
?
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Ala-Ala-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Ala-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-tosyl-Gly-Pro-Lys + p-nitroaniline
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
N-tosyl-L-Lys methyl ester + H2O
N-tosyl-L-Lys + methanol
native hemoglobin + H2O
?
-
-
-
-
?
oxidized insulin B chain + H2O
?
pepsin soluble collagen + H2O
?
-
from the cartilages of brownbanded bamboo shark Chiloscyllium punctatum and blacktip shark Carcharhinus limbatus
-
-
?
phosphoglycerate kinase + H2O
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
porcine pepsin-solubilised collagen + H2O
?
-
is more resistant to hydrolysis compared with albacore tuna pepsin-solubilised collagen
-
-
?
pyroglutamyl-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn + H2O
pyroglutamyl-Ala-Lys + Ser-Gln-Gly-Gly-Ser-Asn
-
i.e. serum thymic factor
-
-
?
serum thymic factor + H2O
?
-
cleavage of the Lys-Ser bond
-
-
?
single-chain human insulin-like peptide 5 precursor + H2O
two-chain human insulin-like peptide 5
-
endoproteinase Lys-C can cleave the peptide bond at the C-terminal side of lysine residues
-
-
?
somatropin + H2O
?
-
protein digested with either trypsin or endoproteinase Lys-C prior to MALDI-MS analysis as a rapid method based on MALDI-TOF-MS peptide mass finger printing for identification of somatropin: sequence coverage obtained from individual trypsin and Lys-C is 79% and 60%, respectively, sequence coverage of both maps together is 98%
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Ala-Ala-Lys + 7-amino-4-methylcoumarin
-
-
-
?
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Ala-Lys + 7-amino-4-methylcoumarin
-
-
-
?
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Lys + 7-amino-4-methylcoumarin
-
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
Trypsinogen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
from calf skin
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr + H2O
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys + Val-Val-Thr
-
i.e. dynorphin B
-
?
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr + H2O
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys + Ser-Gln-Thr-Pro-Leu-Val-Thr
-
i.e. alpha-endorphin
-
?
Val-Leu-Lys-p-nitroanilide + H2O
Val-Leu-Lys + p-nitroaniline
-
-
-
-
?
yellowfin tuna pepsin-solubilised collagen + H2O
?
-
undergoes hydrolysis to the highest extent
-
-
?
additional information
?
-
50S ribosomal protein L7/L12 + H2O
?
cleavage into 5 peptide fragments
-
-
?
50S ribosomal protein L7/L12 + H2O
?
cleavage into 5 peptide fragments
-
-
?
6-phosphogluconate dehydrogenase + H2O
?
cleavage into 7 peptide fragments
-
-
?
6-phosphogluconate dehydrogenase + H2O
?
cleavage into 6 peptide fragments
-
-
?
acyl carrier protein + H2O
?
cleavage into 3 peptide fragments
-
-
?
acyl carrier protein + H2O
?
cleavage into 3 peptide fragments
-
-
?
amyloid beta-protein + H2O
?
only the Lys-X bond is hydrolyzed
-
?
amyloid beta-protein + H2O
?
only the Lys-X bond is hydrolyzed
-
?
B-chain of insulin + H2O
?
-
only cleavage of the bond Lys29-Ala30
-
-
?
B-chain of insulin + H2O
?
-
protease I1 cleaves Lys29-Ala30 bond
-
-
?
B-chain of insulin + H2O
?
-
protease I1 cleaves Lys29-Ala30 bond
-
-
?
B-chain of insulin + H2O
?
-
only cleavage of the bond Lys29-Ala30
-
-
?
benzoyl-L-Lys-4-nitroanilide + H2O
benzoyl-L-Lys + 4-nitroaniline
-
-
-
?
benzoyl-L-Lys-4-nitroanilide + H2O
benzoyl-L-Lys + 4-nitroaniline
-
-
-
?
benzoyl-Lys methyl ester + H2O
benzoyl-Lys + methanol
-
-
-
-
?
benzoyl-Lys methyl ester + H2O
benzoyl-Lys + methanol
-
-
?
benzoyl-Lys methyl ester + H2O
benzoyl-Lys + methanol
-
-
?
benzoyl-Lys-p-nitroanilide + H2O
benzoyl-Lys + p-nitroaniline
-
-
-
-
?
benzoyl-Lys-p-nitroanilide + H2O
benzoyl-Lys + p-nitroaniline
-
-
?
casein + H2O
?
-
-
-
-
?
chaperone protein DNA kinase + H2O
?
cleavage into 10 peptide fragments
-
-
?
chaperone protein DNA kinase + H2O
?
cleavage into 9 peptide fragments
-
-
?
elongation factor G + H2O
?
cleavage into 8 peptide fragments
-
-
?
elongation factor G + H2O
?
cleavage into 5 peptide fragments
-
-
?
elongation factor Tu + H2O
?
cleavage into 7 peptide fragments
-
-
?
elongation factor Tu + H2O
?
cleavage into 5 peptide fragments
-
-
?
enolase + H2O
?
cleavage into 4 peptide fragments
-
-
?
enolase + H2O
?
cleavage into 4 peptide fragments
-
-
?
fructose-bisphosphate aldolase class 2 + H2O
?
cleavage into 5 peptide fragments
-
-
?
fructose-bisphosphate aldolase class 2 + H2O
?
cleavage into 4 peptide fragments
-
-
?
Glucagon + H2O
?
only the Lys-X bond is hydrolyzed
-
?
Glucagon + H2O
?
specific hydrolysis of lysyl peptide bond
-
-
?
Glucagon + H2O
?
specific hydrolysis of lysyl peptide bond
-
-
?
Glucagon + H2O
?
only the Lys-X bond is hydrolyzed
-
?
glyceraldehyde-3-phosphate dehydrogenase A + H2O
?
cleavage into 5 peptide fragments
-
-
?
glyceraldehyde-3-phosphate dehydrogenase A + H2O
?
cleavage into 6 peptide fragments
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
slow reaction
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
slow reaction
-
-
?
Lys-p-nitroanilide + H2O
Lys + p-nitroaniline
-
-
-
-
?
Lys-p-nitroanilide + H2O
Lys + p-nitroaniline
-
-
-
-
?
lysine vasopressin + H2O
?
-
only the Lys8-Gly9 bond is hydrolyzed
-
-
?
lysine vasopressin + H2O
?
-
only the Lys8-Gly9 bond is hydrolyzed
-
-
?
N-benzoyl-L-Lys-p-nitroanilide + H2O
N-benzoyl-L-Lys + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-Lys-p-nitroanilide + H2O
N-benzoyl-L-Lys + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-Lys-p-nitroanilide + H2O
N-benzoyl-L-Lys + p-nitroaniline
-
-
-
-
?
N-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
-
?
N-tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
N-tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
-
?
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
-
-
-
-
?
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
-
-
-
-
?
N-tosyl-L-Lys methyl ester + H2O
N-tosyl-L-Lys + methanol
-
-
-
-
?
N-tosyl-L-Lys methyl ester + H2O
N-tosyl-L-Lys + methanol
-
-
-
-
?
N-tosyl-L-Lys methyl ester + H2O
N-tosyl-L-Lys + methanol
-
-
-
-
?
oxidized insulin B chain + H2O
?
only the Lys-X bond is hydrolyzed
-
?
oxidized insulin B chain + H2O
?
only the Lys-X bond is hydrolyzed
-
?
phosphoglycerate kinase + H2O
?
cleavage into 4 peptide fragments
-
-
?
phosphoglycerate kinase + H2O
?
cleavage into 4 peptide fragments
-
-
?
Substance P + H2O
?
-
hydrolysis of the bond Lys3-Pro4
-
-
?
Substance P + H2O
?
-
hydrolysis of the bond Lys3-Pro4
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
a chromogenic substrate
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
a chromogenic substrate
-
-
?
tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
tosyl-Gly-Pro-Lys + 4-nitroaniline
-
a chromogenic substrate
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Lys-p-nitroanilide + H2O
tosyl-Gly-Pro-Lys + p-nitroaniline
-
-
-
-
?
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
-
-
?
tosyl-Lys methyl ester + H2O
tosyl-Lys + methanol
-
-
-
-
?
additional information
?
-
-
the enzyme cleaves only the Lys-X bond
-
-
?
additional information
?
-
-
the enzyme cleaves only the Lys-X bond
-
-
?
additional information
?
-
-
the enzyme cleaves only the Lys-X bond
-
-
?
additional information
?
-
-
no hydrolysis of: N-benzoyl-L-Arg p-nitroanilide and Arg-p-nitroanilide
-
-
?
additional information
?
-
-
peptide maps of those collagens from both shark species digested by lysyl endopeptidase are different and are completely different from those of type I collagen from calf skin: calf skin collagen is more susceptible to hydrolysis by lysyl endopeptidase than acid soluble collagen or pepsin soluble collagen from both shark cartilages, possibly due to the higher amount of lysine residues in calf skin collagen
-
-
?
additional information
?
-
-
the peptide maps of different pepsin-solubilised collagens hydrolysed by lysyl endopeptidase are different, suggesting that there may be some differences in their primary structures, especially the alpha-helix strand, in terms of sequence as well as amino acid composition
-
-
?
additional information
?
-
-
neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A
-
-
?
additional information
?
-
the enzyme is specific for the C-terminal side of lysine residues, protein and peptide digestion efficiency, usage of quantitative mass spectrometry, analysis of miscleavage and non-cleavage, overview
-
-
?
additional information
?
-
-
neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A
-
-
?
additional information
?
-
-
no hydrolysis of: N-benzoyl-L-Arg p-nitroanilide and Arg-p-nitroanilide
-
-
?
additional information
?
-
-
the enzyme cleaves only the Lys-X bond
-
-
?
additional information
?
-
-
the enzyme cleaves only the Lys-X bond
-
-
?
additional information
?
-
-
the enzyme cleaves only the Lys-X bond
-
-
?
additional information
?
-
-
endoproteinase lysine-C (Lys-C) can specifically identify and cleave C-terminal lysine with high efficiency and specificity
-
-
?
additional information
?
-
-
endoproteinase lysine-C (Lys-C)/trypsin sequential digestion can be used in human 293T cell proteomics sample preparation, evaluation of the advantages of Lys-C/trypsin sequential digestion over trypsin digestion in solution conditions in different aspects, method optimzation, 2 M urea and trypsin in 50:1 or 100:1 ratio, overview. The peptides obtained by sequential digestion are of proper length and can be easily extracted from the gel so as to be more suitable for mass spectrometric identification
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
the enzyme is specific for the C-terminal side of lysine residues, protein and peptide digestion efficiency, usage of quantitative mass spectrometry, analysis of miscleavage and non-cleavage, overview
-
-
?
additional information
?
-
no activity with benzoyl-Arg-p-nitroanilide, Arg-p-nitroanilide, succinyl-Ala-p-nitroanilide, tert-butyloxycarbonyl-His-p-nitroanilide, acetyl-Phe-p-nitroanilide, benzoyl-Tyr-p-nitroanilide and acetyl-Leu-p-nitroanilide
-
?
additional information
?
-
-
no activity with benzoyl-Arg-p-nitroanilide, Arg-p-nitroanilide, succinyl-Ala-p-nitroanilide, tert-butyloxycarbonyl-His-p-nitroanilide, acetyl-Phe-p-nitroanilide, benzoyl-Tyr-p-nitroanilide and acetyl-Leu-p-nitroanilide
-
?
additional information
?
-
no activity with benzoyl-Arg-p-nitroanilide, Arg-p-nitroanilide, succinyl-Ala-p-nitroanilide, tert-butyloxycarbonyl-His-p-nitroanilide, acetyl-Phe-p-nitroanilide, benzoyl-Tyr-p-nitroanilide and acetyl-Leu-p-nitroanilide
-
?
additional information
?
-
Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin is a poor substrate
-
-
?
additional information
?
-
the enzyme has a Lys-specific serine endopeptidase activity and requires processing by cysteine protease Rgp for its activation
-
-
?
additional information
?
-
-
strict specificity: only peptide, ester, and amide bonds containing the carbonyl group of lysine are hydrolyzed
-
-
?
additional information
?
-
-
the enzyme inhibits four host cell surfactant-associated proteins designated SP-A, SP-B, SP-C, and SP-D, degradation of SPs by protease IV inhibits their ability to enhance bacterial association with alveolar macrophages, overview
-
-
?
additional information
?
-
-
the enzyme is a corneal virulence factor of Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
the enzyme is a corneal virulence factor of Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
the enzyme inhibits four host cell surfactant-associated proteins designated SP-A, SP-B, SP-C, and SP-D, degradation of SPs by protease IV inhibits their ability to enhance bacterial association with alveolar macrophages, overview
-
-
?
additional information
?
-
-
Chinese hamster ovary-expressed monoclonal antibody subjected to limited digestion using the endoproteinase Lys-C and reduced to generate Fab heavy chain, single chain Fc and light chain fragments (ca. 25 kDa each)
-
-
?
recombinant beta2-microglobulin + H2O
additional information
-
-
-
production of nine peptides: K1 (Glu4-Lys6), K2 (Ile7-lys19), K3 (Ser20-Lys41), K4 (Asn42-Lys48), K5 (Val49-Lys58), K6 (Asp59-Lys75), K7 (Asp76-Lys91), K8 (Ile92-Lys94), and K9 (Trp95-Met99). K3 and K7 are linked by a disulfide bond between Cys25 and Cys80
?
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20
benzoyl-Arg ethyl ester
-
-
0.091
benzoyl-Lys methyl ester
-
-
0.08 - 0.11
Lys-p-nitroanilide
1.59
N-acetyl-L-lysine
-
pH 9, rate of carboxyl oxygen exchange reaction by Lys-C is accelerated at acidic pH conditions.
0.07 - 0.09
N-benzoyl-L-Lys p-nitroanilide
0.63 - 1
N-benzoyl-L-Orn methyl ester
3.09
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide
-
-
3.11
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide
-
-
41
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide
-
-
0.034
N-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
2.5 - 35.7
N-tosyl-L-Arg methyl ester
0.053 - 0.1
N-tosyl-L-Lys methyl ester
0.0028 - 0.024
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
0.0037 - 0.042
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
0.029 - 0.081
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
0.0007 - 0.032
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
0.034 - 0.25
tosyl-Gly-Pro-Lys-p-nitroanilide
0.053
Tosyl-Lys methyl ester
-
pH 8.0
0.33
Val-Leu-Lys-p-nitroanilide
-
-
0.08
Lys-p-nitroanilide
-
-
0.08
Lys-p-nitroanilide
-
protease I
0.11
Lys-p-nitroanilide
-
protease Ia
0.07
N-benzoyl-L-Lys p-nitroanilide
-
-
0.07
N-benzoyl-L-Lys p-nitroanilide
-
protease I
0.09
N-benzoyl-L-Lys p-nitroanilide
-
protease Ia
0.63
N-benzoyl-L-Orn methyl ester
-
protease Ia
1
N-benzoyl-L-Orn methyl ester
-
-
1
N-benzoyl-L-Orn methyl ester
-
protease I
2.5
N-tosyl-L-Arg methyl ester
-
protease Ia
35.7
N-tosyl-L-Arg methyl ester
-
-
35.7
N-tosyl-L-Arg methyl ester
-
protease I
0.053
N-tosyl-L-Lys methyl ester
-
-
0.083
N-tosyl-L-Lys methyl ester
-
protease Ia
0.1
N-tosyl-L-Lys methyl ester
-
-
0.1
N-tosyl-L-Lys methyl ester
-
protease I
0.0028
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
0.004
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
0.0046
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
0.006
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210S
0.0061
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
0.0063
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
0.01
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
0.012
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
0.023
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
0.024
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
0.0037
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
0.0058
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
0.0072
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
0.0099
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
0.034
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
0.034
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
0.042
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
0.029
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
0.037
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
0.038
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
0.046
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
0.066
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
0.074
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
0.081
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
0.0007
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210S
0.0013
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
0.0021
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
0.0034
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
0.0036
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
0.0043
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
0.0073
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
0.01
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
0.017
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
0.02
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
0.032
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169G
0.034
tosyl-Gly-Pro-Lys-p-nitroanilide
-
pH 9.0
0.25
tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.41
benzoyl-Arg ethyl ester
-
-
225
benzoyl-Lys methyl ester
-
-
0.86
benzoyl-Lys-p-nitroanilide
-
-
0.14
Lys-p-nitroanilide
-
-
10.4
N-benzoyl-L-Orn methyl ester
-
-
49
N-tert-butyloxycarbonyl-Ala-Ala-Lys-4-methylcoumarin 7-amide
-
-
32.9
N-tert-butyloxycarbonyl-Ala-Lys-4-methylcoumarin 7-amide
-
-
3.02
N-tert-butyloxycarbonyl-Lys-4-methylcoumarin 7-amide
-
-
59
N-tosyl-Gly-Pro-Lys-p-nitroanilide
-
-
5.04
N-tosyl-L-Arg methyl ester
-
-
282 - 570
N-tosyl-L-Lys methyl ester
2.6 - 98
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
1.1 - 46
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
0.4 - 8.4
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
0.8 - 96
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
59
tosyl-Gly-Pro-Lys-p-nitroanilide
-
pH 9.0
282
Tosyl-Lys methyl ester
-
pH 8.0
282
N-tosyl-L-Lys methyl ester
-
-
570
N-tosyl-L-Lys methyl ester
-
-
2.6
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
15
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
18
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210S
20
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
23
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
37
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
40
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
48
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
51
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
98
tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
1.1
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
7
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
11
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
22
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
24
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
31
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
46
tert-butyloxycarbonyl-Ala-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
0.4
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
2.3
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
2.7
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
4.5
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
5.2
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
6
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
8.4
tert-butyloxycarbonyl-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
0.8
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169G
2 - 8
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169V
3 - 6
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169L
4.6
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169A
45
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
52
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210S
67
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169H
71
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169F
83
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme W169Y
93
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, wild-type enzyme
96
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 9.0, 37°C, mutant enzyme H210A
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H210/W169F
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 8.6% of the wild-type ratio
H210A/W169A
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 0.25% of the wild-type ratio
H210F
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin is 14% of the wild-type value, the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 29.5% of the wild-type value
H210K
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 0.02% of the wild-type ratio
W169G
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 0.06% of the wild-type value
H210A
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin is 7.1% of the wild-type value, the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is identical to the wild-type value
H210A
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 80% of the wild-type ratio
H210S
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Ala-Ala-Lys-7-amido-4-methylcoumarin is 8.6% of the wild-type value, the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 1.7fold higher than the wild-type value
H210S
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 1.7fold higher than the wild-type ratio
H210S
crystallization data. Optimum pH value shifts from around pH 9 of wild-type to approximately pH 7, while retaining high activity
W169A
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate 0.5% of the wild-type ratio
W169A
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 0.5% of the wild-type value
W169F
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 43% of the wild-type ratio
W169F
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 45% of the wild-type value
W169F
crystallization data. Optimum pH value shifts from around pH 9 of wild-type to approximately pH 7, while retaining high activity
W169H
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 9% of the wild-type ratio
W169H
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 9% of the wild-type value
W169L
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 25% of the wild-type ratio
W169L
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 25% of the wild-type value
W169V
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 6% of the wild-type ratio
W169V
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 6% of the wild-type value
W169Y
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin as substrate is 43% of the wild-type ratio
W169Y
-
the ratio of turnover number to Km-value for tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin is 43% of the wild-type value
Q520S
-
site-directed mutagenesis, the mutant shows altered substrate binding compared to the wild-type enzyme
Q520S
-
site-directed mutagenesis, the mutant shows altered substrate binding compared to the wild-type enzyme
-
additional information
-
generation of a Gly681-Ala710 deletion mutant
additional information
-
generation of a Gly681-Ala710 deletion mutant
-
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Masaki, T.; Suzuki, H.; Soejima, M.
Purification and some properties of Achromobacter protease Ia from Achromobacter lyticus M497-1
Agric. Biol. Chem.
50
3087-3091
1986
Achromobacter lyticus, Achromobacter lyticus M497-1
-
brenda
Morihara, K.; Muneyuki, R.; Oka, T.
Use of immobilized Achromobacter protease I for semisynthesis of human insulin
Methods Enzymol.
136
162-170
1987
Achromobacter lyticus
brenda
Masaki, T.; Soejima, M.
Actions of Achromobacter protease I on some zymogens and dimethylcasein
Agric. Biol. Chem.
49
1867-1868
1985
Achromobacter lyticus
-
brenda
Masaki, T.; Fujihashi, T.; Nakamura, K.; Soejima, M.
Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I
Biochim. Biophys. Acta
660
51-55
1981
Achromobacter lyticus, Achromobacter lyticus M497-1
brenda
Masaki, T.; Tanabe, M.; Nakamura, K.; Soejima, M.
Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties
Biochim. Biophys. Acta
660
44-50
1981
Achromobacter lyticus, Achromobacter lyticus M497-1
brenda
Masaki, T.; Nakamura, T.; Isono, M.; Soejima, M.
A new proteolytic enzyme from Achromobacter lyticus M497-1
Agric. Biol. Chem.
42
1443-1445
1978
Achromobacter lyticus, Achromobacter lyticus M497-1
-
brenda
Oda, Y.; Kitagawa, Y.; Yamaguchi, H.; Matsuura, Y.; Katsube, Y.; Masaki, T.; Tanaka, T.; Matsuura, S.; Norioka, S.
Crystallization and preliminary X-ray diffraction analysis of two lysinal derivatives of Achromobacter protease I
Acta Crystallogr. Sect. D
52
1027-1029
1996
Achromobacter lyticus, Achromobacter lyticus M497-1
brenda
Leonard, R.B.; Carroll, K.C.
Rapid lysis of gram-positive cocci for pulsed-field gel electrophoresis using achromopeptidase
Diagn. Mol. Pathol.
6
288-291
1997
Achromobacter lyticus
brenda
Masaki, T.; Tanaka, T.; Tsunasawa, S.; Sakiyama, F.; Soejima, S.
Inhibition of Achromobacter protease I by lysinal derivatives
Biosci. Biotechnol. Biochem.
56
1604-1607
1992
Achromobacter lyticus
brenda
Jekel, P.A.; Weijer, W.J.; Beintema, J.J.
Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis
Anal. Biochem.
134
347-354
1983
Lysobacter enzymogenes
brenda
Fujimura, S.; Shibata, Y.; Nakamura, T.
Purification and partial characterization of a lysine-specific protease of Porphyromonas gingivalis
FEMS Microbiol. Lett.
113
133-138
1993
Porphyromonas gingivalis
brenda
Ohara, T.; Makino, K.; Shinagawa, H.; Nakata, A.; Norioka, S.; Sakiyama, F.
Cloning, nucleotide sequence, and expression of Achromobacter protease I gene
J. Biol. Chem.
264
20625-20631
1989
Achromobacter lyticus
brenda
Elliott, B.W.; Cohen, C.
Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa
J. Biol. Chem.
261
11259-11265
1986
Pseudomonas aeruginosa
brenda
Tsunasawa, S.; Masaki, T.; Hirose, M.; Soejima, M.; Sakiyama, F.
The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease
J. Biol. Chem.
264
3832-3839
1989
Achromobacter lyticus
brenda
Sakiyama, F.; Masaki, T.
Lysyl endopeptidase of Achromobacter lyticus
Methods Enzymol.
244
126-137
1994
Achromobacter lyticus
brenda
Shiraki, K.; Norioka, S.; Li, S.; Yokota, K.; Sakiyama, F.
Electrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease,Achromobacter protease I
Eur. J. Biochem.
269
4152-4158
2002
Achromobacter lyticus
brenda
Chohnan, S.; Nonaka, J.; Teramoto, K.; Taniguchi, K.; Kameda, Y.; Tamura, H.; Kurusu, Y.; Norioka, S.; Masaki, T.; Sakiyama, F.
Lysobacter strain with high lysyl endopeptidase production
FEMS Microbiol. Lett.
213
13-20
2002
Lysobacter sp. (Q9AQR5), Lysobacter sp., Lysobacter sp. IB-9374 (Q9AQR5)
brenda
Shiraki, K.; Norioka, S.; Li, S.; Sakiyama, F.
Contribution of an imidazole-indole stack to high catalytic potency of a lysine-specific serine protease, Achromobacter protease I
J. Biochem.
131
213-218
2002
Achromobacter lyticus
brenda
Kozhukh, G.V.; Hagihara, Y.; Kawakami, T.; Hasegawa, K.; Naiki, H.; Goto, Y.
Investigation of a peptide responsible for amyloid fibril formation of beta2-microglobulin by Achromobacter protease I
J. Biol. Chem.
277
1310-1315
2002
Achromobacter lyticus
brenda
Chohnan, S.; Shiraki, K.; Yokota, K.; Ohshima, M.; Kuroiwa, N.; Ahmed, K.; Masaki, T.; Sakiyama, F.
A second lysine-specific serine protease from Lysobacter sp. strain IB-9374
J. Bacteriol.
186
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2004
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