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5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu-Arg + H2O
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu + Arg
-
-
-
?
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine + H2O
?
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu + Ala
-
-
-
-
?
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine + H2O
?
-
-
-
-
?
acetyl-Phe ethyl ester + H2O
?
-
-
-
-
?
acetyl-Phe-Leu + H2O
acetyl-Phe + Leu
-
-
-
-
?
acetyl-Phe-NH2 + H2O
?
-
-
-
-
?
Acetyl-Tyr ethyl ester + H2O
?
-
-
-
-
?
acetyl-Tyr-ethyl ester + H2O
?
-
-
-
-
?
adrenocorticotropic hormone fragment 7-38 + H2O
?
-
-
-
-
?
benzoyl-Ala benzyl ester + H2O
?
-
-
-
-
?
benzoyl-Ala-OGly + H2O
?
-
-
-
-
?
benzoyl-Ala-OMe + H2O
?
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitrolaniline
benzoyl-Gly benzyl ester + H2O
?
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
benzoyl-Gly-beta-phenyllactate + H2O
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
isoenzyme MpiCP-2
-
-
?
benzoyl-Gly-OEt + H2O
?
-
-
-
-
?
benzoyl-Gly-OGly + H2O
?
-
-
-
-
?
benzoyl-Gly-OMe + H2O
?
-
-
-
-
?
benzoyl-Gly-OPhe + H2O
?
-
-
-
-
?
benzoyl-Gly-Phe + H2O
benzoyl-Gly + Phe
-
-
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
benzoyl-L-tyrosine-p-nitroanilide + H2O
benzoyl-L-tyrosine + p-nitroaniline
-
-
-
-
?
benzoyl-Phe-Gly + H2O
benzoyl-Phe + Gly
-
-
-
-
?
benzoyl-Phe-OGly + H2O
?
-
-
-
-
?
benzoyl-Phe-OMe + H2O
?
-
-
-
-
?
benzoyl-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala + H2O
benzyloxycarbonyl-Ala + Ala
-
-
-
-
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
Benzyloxycarbonyl-Ala-Leu + H2O
Benzyloxycarbonyl-Ala + Leu
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
-
-
-
-
?
benzyloxycarbonyl-Arg-Pro + H2O
benzyloxycarbonyl-Arg + Pro
Citrus sp.
-
-
-
-
?
benzyloxycarbonyl-Glu-Leu + H2O
benzyloxycarbonyl-Glu + Leu
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
benzyloxycarbonyl-Gly-Arg + H2O
benzyloxycarbonyl-Gly + Arg
-
-
-
-
?
benzyloxycarbonyl-Gly-Glu + H2O
benzyloxycarbonyl-Gly + Glu
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
benzyloxycarbonyl-Gly-Gly + Phe
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
benzyloxycarbonyl-Gly-Met + H2O
benzyloxycarbonyl-Gly + Met
-
19% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
benzyloxycarbonyl-Gly-Pro + H2O
benzyloxycarbonyl-Gly + Pro
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
benzyloxycarbonyl-Gly-Pro-Leu-Gly + Pro
-
3% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Gly-Val + H2O
Benzyloxycarbonyl-Gly + Val
-
24% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-His-Leu + H2O
benzyloxycarbonyl-His + Leu
-
-
-
-
?
benzyloxycarbonyl-His-Phe + H2O
benzyloxycarbonyl-His + Phe
-
-
-
-
?
benzyloxycarbonyl-His-Tyr + H2O
benzyloxycarbonyl-His + Tyr
-
-
-
-
?
benzyloxycarbonyl-Ile-Leu + H2O
benzyloxycarbonyl-Ile + Leu
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Leu + H2O
benzyloxycarbonyl-L-Phe + L-Leu
-
-
-
?
benzyloxycarbonyl-L-phenylalanyl-L-leucine + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
?
benzyloxycarbonyl-Leu-Leu + H2O
benzyloxycarbonyl-Leu + Leu
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
benzyloxycarbonyl-Nle-Leu + H2O
benzyloxycarbonyl-Nle + Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
benzyloxycarbonyl-Phe-beta-Ala + H2O
benzyloxycarbonyl-Phe + beta-Ala
-
-
-
-
?
benzyloxycarbonyl-Phe-Glu + H2O
benzyloxycarbonyl-Phe + Glu
-
-
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
benzyloxycarbonyl-Phe-His + H2O
benzyloxycarbonyl-Phe + His
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
benzyloxycarbonyl-Phe-NH2 + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Phe + H2O
benzyloxycarbonyl-Phe + Phe
-
-
-
-
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
benzyloxycarbonyl-Phe-Tyr-Gly + H2O
benzyloxycarbonyl-Phe-Tyr + Gly
-
172% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Tyr-Leu + H2O
benzyloxycarbonyl-Phe-Tyr + Leu
-
120% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Pro-Leu + H2O
benzyloxycarbonyl-Pro + Leu
-
-
-
-
?
benzyloxycarbonyl-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Pro-Leu + Gly
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Ser-Leu + H2O
benzyloxycarbonyl-Ser + Leu
-
-
-
-
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
benzyloxycarbonyl-Tyr-Gly + H2O
benzyloxycarbonyl-Tyr + Gly
-
188% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Tyr-Phe + H2O
benzyloxycarbonyl-Tyr + Phe
-
201% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Val-Leu + H2O
benzyloxycarbonyl-Val + Leu
-
-
-
-
?
bombesin + H2O
?
-
-
-
-
?
carboxypropionyl-Phe-4-nitroanilide + H2O
carboxypropionyl-Phe + 4-nitroaniline
CBZ-Phe-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-leucine
-
-
-
?
corn gluten + H2O
?
-
-
-
-
?
corticotropin-releasing factor fragment 6-33 + H2O
?
-
-
-
-
?
cyclo-statherin Q-37 + H2O
?
-
-
-
-
?
endothelin + H2O
?
-
-
-
-
?
endothelin I + H2O
endothelin(1-20) + Trp
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
furylacryloyl-Ala-Glu + H2O
furylacryloyl-Ala + Glu
-
-
-
-
?
furylacryloyl-Ala-Leu + H2O
furylacryloyl-Ala + Leu
-
-
-
-
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
furylacryloyl-Arg-Leu + H2O
furylacryloyl-Arg + Leu
-
preferred substrate
-
-
?
furylacryloyl-Lys-Ala + H2O
furylacryloyl-Lys + Ala
-
-
-
-
?
furylacryloyl-Lys-Leu + H2O
furylacryloyl-Lys + leu
-
-
-
-
?
furylacryloyl-Phe ethyl ester + H2O
?
-
-
-
-
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
furylacryloyl-Phe-Gly + H2O
?
-
-
-
-
?
furylacryloyl-Phe-Leu + H2O
?
-
-
-
-
?
furylacryloyl-Phe-Leu + H2O
furylacryloyl-Phe + Leu
-
-
-
-
?
furylacryloyl-Phe-NHEt + H2O
?
-
-
-
-
?
furylacryloyl-Phe-OGly + H2O
?
-
-
-
-
?
furylacryloyl-Phe-OGly-OH + H2O
?
-
-
-
-
?
furylacryloyl-Phe-OMe + H2O
?
-
-
-
-
?
furylacryloyl-Phe-Phe + H2O
furylacryloyl-Phe + Phe
-
-
-
-
?
furylacryloyl-Phe-Val + H2O
furylacryloyl-Phe + Val
-
-
-
-
?
FVNQHLCGSHLV + H2O
FVNQHLCGSH + L-Leu-L-Val + L-Val
-
-
-
-
?
FVNQHLCGSHLVEAL + H2O
FVNQHLCGSHLVE + L-Ala-L-Leu + L-Leu
-
-
-
-
?
Glu-Asp-Glu-Phe-Phe-Leu-Ala + H2O
Glu-Asp-Glu-Phe-Phe-Leu + Ala
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
hippuryl-beta-phenyl lactate + H2O
?
-
-
-
-
?
isoaspartyl peptides + H2O
isoaspartyl dipeptides
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
lysosomal neuraminidase-1 + H2O
?
lysosomal neuraminidase-1 gains full catalytic activity in the lysosome through its binding to PPCA
-
-
?
N-((S)-5-amino-5-(carbamoyl)pentyl)-3-(aminooxymethyl)benzamide + H2O
?
-
-
-
?
N-(2-furanacryloyl)-Phe-Phe + H2O
N-(2-furanacryloyl)-Phe + Phe
-
-
-
-
?
N-(4-methoxyphenyl-azoformyl)-L-Phe-OH + H2O
?
-
-
-
-
?
N-acetyl-renin tetradecapeptide + H2O
?
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-Tyr + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
N-carbobenzoxy-L-Phe-L-Ala + H2O
N-carbobenzoxy-L-Phe + L-Ala
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha
oxidized insulin B + H2O
?
-
-
-
-
?
pancreatic carboxypeptidase A + H2O
hydrolyzed carboxypeptidase A + C-terminal amino acid
-
-
-
?
pancreatic carboxypeptidase B + H2O
hydrolyzed pancreatic carboxypeptidase B + C-terminal amino acid
-
-
-
?
pepsin-digested soy protein + H2O
?
-
-
-
-
?
phytochelatin + H2O
phytochelatin 2 + ?
poly-alpha-L-aspartic acid + H2O
?
-
slowly
-
-
?
poly-alpha-L-glutamic acid + H2O
glutamic acid
-
-
-
?
succinyl-L-Ile-L-Ile-L-Trp-7-amido-4-methylcoumarin + H2O
succinyl-L-Ile-L-Ile-L-Trp + 7-amino-4-methylcoumarin
-
-
-
-
?
Tamm-Horsfall glycoprotein + H2O
?
-
-
-
-
?
trypsin-digested casein + H2O
?
-
-
-
-
?
additional information
?
-
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitrolaniline
Citrus sp.
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitrolaniline
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
isoenzyme MpiCP-2
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
benzoyl-Gly-beta-phenyllactate + H2O
?
-
-
-
-
?
benzoyl-Gly-beta-phenyllactate + H2O
?
-
poor substrate
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
-
isoenzyme MpiCP-1
-
-
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
-
76% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
isoenzyme MpiCP-1
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
119% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
150% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
isoenzyme MpiCP-1
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
isoenzyme MpiCP-2
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
-
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
-
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
100% activity
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
17% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
-
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
poor substrate
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
21% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
-
59% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
-
309% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
Citrus sp.
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
isoenzyme MpiCP-1
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
77% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
219% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
24% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
isoenzyme MpiCP-1
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
21% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
483% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
-
-
-
-
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
-
12% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
-
18% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
-
114% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
-
preferred substrate for isoenzyme MpiCP-1
-
-
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
-
preferred substrate for isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
-
134% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
carboxypropionyl-Phe-4-nitroanilide + H2O
carboxypropionyl-Phe + 4-nitroaniline
Citrus sp.
-
-
-
-
?
carboxypropionyl-Phe-4-nitroanilide + H2O
carboxypropionyl-Phe + 4-nitroaniline
-
-
-
-
?
endothelin I + H2O
endothelin(1-20) + Trp
-
containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
-
-
?
endothelin I + H2O
endothelin(1-20) + Trp
-
containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
-
-
-
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
-
-
-
-
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
-
-
-
-
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
-
-
-
-
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Citrus sp.
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha
-
-
-
-
?
phytochelatin + H2O
phytochelatin 2 + ?
-
-
-
-
?
phytochelatin + H2O
phytochelatin 2 + ?
-
-
-
-
?
additional information
?
-
-
BRS1 may be involved in an early proteolytic step important for brassinosteroid perception
-
-
?
additional information
?
-
Citrus sp.
-
-
-
-
?
additional information
?
-
Citrus sp.
-
splits off most readily aromatic and aliphatic amino acid residues at the carboxyl end
-
-
?
additional information
?
-
Citrus sp.
-
removes C-terminal aromatic, neutral acid and basic amino acids, proline bonds are hydrolyzed on both the amino and carboxyl side, glycine is attacked slowly
-
-
?
additional information
?
-
Citrus sp.
-
catalytic mechanism specificity overview
-
-
?
additional information
?
-
Citrus sp.
-
owing to its low specificity very suitable for sequence analysis
-
-
?
additional information
?
-
Citrus sp.
-
glycine is split off very slowly
-
-
?
additional information
?
-
Citrus sp.
-
rapid release of: Phe, Tyr, Trp, Leu, Ile, Val, His, good release of: Ser, Thr, Met, Ala, Asp, Asn, Glu, Gln, Lys, Arg, Pro, S-carboxymethylcysteine, slow release: Gly, no release of: hydroxyproline, D-amino acids. The enzyme requires a free alpha-carboxyl group for action, only L-amino acids are cleaved. The cleavage is strongly influenced by the nature of the penultimate amino acid
-
-
?
additional information
?
-
Citrus sp.
-
no hydrolysis of benzyloxycarbonyl-Gly-Pro
-
-
?
additional information
?
-
Citrus sp.
-
neutral, basic and acid amino acids including proline are all hydrolyzed to approximately the same extent
-
-
?
additional information
?
-
-
catalytic mechanism specificity overview
-
-
?
additional information
?
-
-
does not cleave the MBPMu4 peptide VVHPFPPIVTPPPP
-
-
?
additional information
?
-
-
cis regulation of serine carboxypeptidase I
-
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Gly-Phe, benzyloxycarbonyl-Gly-Pro, benzyloxycarbonyl-Gly-Pro-Leu, benzyloxycarbonyl-Gly-Leu-NH2, benzyloxycarbonyl-Gly-Phe-NH2, benzoyl-Gly-Lys, Leu-Gly-Gly
-
-
?
additional information
?
-
-
no activity with benzyloxycarbonylGlu-Phe, benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Gly-Phe, benzyloxycarbonyl-Gly-Pro, benzyloxycarbonyl-Gly-Pro-Leu, benzyloxycarbonyl-Gly-Leu-NH2, benzyloxycarbonyl-Gly-Phe-NH2, Leu-Gly-Gly
-
-
?
additional information
?
-
no proteolytic activity or increased serine carboxypeptidase activity towards artificial serine carboxypeptidase substrates of the purified recombinant 55 kDa precursor and the homogenates of Scpep1-overexpressing cells is detected
-
-
?
additional information
?
-
-
no proteolytic activity or increased serine carboxypeptidase activity towards artificial serine carboxypeptidase substrates of the purified recombinant 55 kDa precursor and the homogenates of Scpep1-overexpressing cells is detected
-
-
?
additional information
?
-
-
Scpep1 has carboxypeptidase activity against endothelin ET-1
-
-
?
additional information
?
-
-
rapid release of: Phe, Tyr, Trp, Leu, Ile, Val, His, good release of: Ser, Thr, Met, Ala, Asp, Asn, Glu, Gln, Lys, Arg, Pro, S-carboxymethylcysteine, slow release: Gly, no release of: hydroxyproline, D-amino acids. The enzyme requires a free alpha-carboxyl group for action, only L-amino acids are cleaved. The cleavage is strongly influenced by the nature of the penultimate amino acid
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
overview: synthetic substrates
-
-
?
additional information
?
-
-
no effect on the activity of malate dehydrogenase
-
-
?
additional information
?
-
-
activity towards substrates with basic P1 amino acid residues is drastically increased by mutational replacement of Leu178
-
-
?
additional information
?
-
-
structural requirements for nucleophilic substrates
-
-
?
additional information
?
-
-
the mechanism involves a charge-relay system in the hydrolysis of peptide and ester substrates
-
-
?
additional information
?
-
-
inactivation of phosphoribosyltransferase
-
-
?
additional information
?
-
-
catalytic mechanism specificity overview
-
-
?
additional information
?
-
-
Asn51 and Glu145 of carboxypeptidase Y each donate a hydrogen bond to the alpha-carboxylate of peptide substrates. The same groups are involved in the interaction with the C-terminal carboxamide group of peptide amides. Asn51 donates a hydrogen bond to the C=O group of the substrate, and Glu145 (in the charged form) accepts one from the NH2 group of the substrate
-
-
?
additional information
?
-
-
substrates overview
-
-
?
additional information
?
-
-
mechanism of carboxypeptidase-Y-catalyzed peptide semisynthesis
-
-
?
additional information
?
-
-
studies on hydrolytic properties
-
-
?
additional information
?
-
-
no hydrolysis of poly-L-lysine
-
-
?
additional information
?
-
-
no hydrolysis of poly-L-proline
-
-
?
additional information
?
-
-
endopeptidase activity is due to the presence of contaminating amounts of yeast proteinase A and caution should by taken when employing carboxypeptidase Y preparations for sequence studies
-
-
?
additional information
?
-
-
the enzyme is involved in the C-terminal processing of peptides and proteins
-
-
?
additional information
?
-
-
the enzyme is involved in the degradation of biologically active peptide amides
-
-
?
additional information
?
-
-
at semipermissive temperatures, carboxypeptidase Y transit time to the vacuole is slower in Sec- cells containing an ire1DELTA or hac1DELTA mutation than in Sec- cells with an intact unfolded protein response pathway
-
-
?
additional information
?
-
-
CPD-Y can be used to specifically modify the C-terminus of peptides and proteins, for example biotinylation of antibodies at their C-termini
-
-
?
additional information
?
-
-
no activity towards benzyloxycarbonyl-Gly-Pro, benzoyl-Gly-Lys, and benzyloxycarbonyl-Pro-Pro
-
-
?
additional information
?
-
-
catalytic mechanism specificity overview
-
-
?
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(3R)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methoxyphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(3-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-[2-(trifluoromethyl)phenyl]propanoic acid
-
-
(3S)-3-(([1-(3-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(3-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([1-(4-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([4-chloro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(([4-fluoro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-(2,4-dichlorophenyl)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
-
-
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
-
-
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
-
-
(3S)-3-([(4-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([(4-methoxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([[5-(cyclopropylmethoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-([[5-ethoxy-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
-
-
(3S)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]-3-(2-methylphenyl)propanoic acid
-
-
(S)-1-chloro-4-phenyl-3-tosylamido-2-butanone
-
37% residual activity at 1 mM
1,2-epoxy-3-(p-nitrophenoxy)propane
-
1 mM, 14% inhibition, isoenzyme MpiCP-2
2,2'-dipyridyl
-
1 mM, 21% inhibition, isoenzyme MpiCP-1; 1 mM, 22% inhibition, isoenzyme MpiCP-2
2-propanol
Citrus sp.
-
above 5%
3,4-dichloroisocoumarin
-
effective inhibitor
3-(([1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-fluorophenyl)propanoic acid
-
-
3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-phenylpropanoic acid
-
-
3-(([1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
-
-
3-(([1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid
-
-
3-(2,3-dichlorophenyl)-3-(([1-(2,4-difluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
-
-
3-(2,3-dichlorophenyl)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)propanoic acid
-
-
3-(4'-fluorobiphenyl-4-yl)-3-([[1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
-
-
3-(5-fluoro-2-methylphenyl)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
-
-
3-(biphenyl-4-yl)-3-([[1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
-
-
3-Phenyl-1-propanol
-
inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe
3-[[(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino]-3-(4-phenoxyphenyl)propanoic acid
-
-
4-Aminobenzylsuccinic acid
-
-
acetyl-D-Phe ethyl ester
-
-
acetyl-D-Phe-ethyl ester
-
-
benzyloxycarbonyl-D-Phe
-
-
benzyloxycarbonyl-D-Phe-D-Leu
-
-
benzyloxycarbonyl-Gly-Leu-Phe-CH2Cl
-
-
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
benzyloxycarbonyl-L-phenylalanyl chloromethane
-
diisopropylphosphorofluoridate-inactivated enzyme does not react with the inhibitor
benzyloxycarbonyl-Phe
-
-
beta-phenyl-L-lactate
-
-
Beta-phenylpropionate
-
-
carboxypeptidase inhibitor IC
-
-
-
carboxypeptidase Y inhibitor from baker's yeast
-
MW 23400-24000, purification, chemical and physical properties
-
carboxypeptidase Y inhibitor IC
-
CoSO4
-
62% residual activity at 10 mM
CuCl
-
1 mM, 37% inhibition
CuCl2
-
1 mM, 39% inhibition
CuSO4
-
4% residual activity at 10 mM
D-Amino acids
-
less inhibitory than the L-enantiomers, non-competitive or mixed-type
diisopropyl fluorophosphate
diisopropylfluorophosphate
E-64
-
1 mM, 10% inhibition, isoenzyme MpiCP-2; 1 mM, 22% inhibition, isoenzyme MpiCP-1
Elastatinal
-
1 mM, 46% inhibition, isoenzyme MpiCP-2
FeCl3
-
1 mM, 92% inhibition
L-amino acids
-
competitive
leupeptin
-
1 mM, 24% inhibition, isoenzyme MpiCP-1; 1 mM, 60% inhibition, isoenzyme MpiCP-2
MnCl2
-
1 mM, 14% inhibition
N-(N-[1-trans-3-carboxyoxiran-2-carbonyl]-L-leucyl)-agmatine
-
93% residual activity at 1 mM
Nalpha-tosyl-L-Lys-chloromethyl ketone
Nalpha-tosyl-L-Phe-chloromethyl ketone
NEM
-
1 mM, 71% inhibition
NH2-blocked amino acids
-
-
-
p-chloromercuribenzenesulfonate
-
-
p-chloromercuribenzoic acid
-
complete inhibition at 1 mM, at 30°C and pH 3.1
p-hydroxymercuribenzene sulfonate
-
mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities
Pb(CH3COO)2
-
60% residual activity at 10 mM
PbCl2
-
1 mM, 95% inhibition
Phe-Asn-Arg-Ala-Val-Asp
-
-
Phe-Asn-Arg-Ala-Val-Val
-
-
Phe-Asn-Arg-Pro-Val-Asp
-
-
Phe-Asn-Arg-Pro-Val-Val
-
-
phenylmethane sulfonylfluoride
-
-
phenylmethylsulfonyl fluoride
-
irreversible
Phenylmethylsulfonylfluoride
phosphoramidon
-
1 mM, 17% inhibition, isoenzyme MpiCP-1; 1 mM, 41% inhibition, isoenzyme MpiCP-2
SDS
-
1 mM, complete inhibition
SnCl2
-
1 mM, complete inhibition
Tfs1p
-
NatB-dependent acetylation is essential for the inhibitory activity on carboxypeptidase Y
-
tosylphenylalanylchloromethane
-
1 mM, 35% inhibition, isoenzyme MpiCP-1
trans-epoxysuccinyl-L-leucylamido-(4-guanidine)-butane
-
-
ZnSO4
-
69% residual activity at 10 mM
2-mercaptoethanol
-
1 mM, 13% inhibition, isoenzyme MpiCP-2
2-mercaptoethanol
-
1 mM, 10% inhibition
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
-
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
irreversible inhibition of peptidase and esterase activity, inhibition is retarded by the competitive inhibitors benzyloxycarbonyl-D-phenylalanine-D-leucine and trans-cinnamate
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
-
CaCl2
-
1 mM, 16% inhibition
CaCl2
-
73% residual activity at 10 mM
carboxypeptidase Y inhibitor IC
-
-
-
carboxypeptidase Y inhibitor IC
-
-
carboxypeptidase Y inhibitor IC
-
-
-
chymostatin
-
IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
chymostatin
-
1 mM, 36% inhibition, isoenzyme MpiCP-1
chymostatin
-
1 mM, 89% inhibition
chymostatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
chymostatin
-
5% residual activity at 1 mM
chymostatin
-
IC50 at pH 5.6: 0.013 mM, IC50 at pH 6.5: 0.0022 mM
Cu+
-
partial
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
Citrus sp.
-
peel enzyme inhibited, leaf enzyme not
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
effective inhibitor
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
benzyloxycarbonyl-L-phenylalanyl chloromethane-inhibited enzyme does not react with the inhibitor
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropylfluorophosphate
-
1 mM, 39% inhibition, isoenzyme MpiCP-1; 1 mM, 67% inhibition, isoenzyme MpiCP-2
diisopropylfluorophosphate
-
1 mM, 63% inhibition
diisopropylfluorophosphate
-
complete inhibition at 5 mM, at 30°C and pH 3.1
ebelactone B
-
IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
ebelactone B
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
ebelactone B
-
IC50: 0.0021 mM (at pH 5.6), IC50: 0.0015 mM (at pH 6.5)
EDTA
-
1 mM, 38% inhibition, isoenzyme MpiCP-1
ethanol
Citrus sp.
-
above 5%
HgCl2
-
1 mM, 54% inhibition
HgCl2
-
complete inhibition at 1 mM, at 30°C and pH 3.1
lactacystin
-
IC50 at pH 5.6: 0.0052 mM, IC50 at pH 6.5: 0.0018 mM
lactacystin
-
CatA is inhibited by 0.03 mM lactacystin
lactacystin
-
IC50 at pH 5.6: 0.048 mM, IC50 at pH 6.5: 0.031 mM
lactacystin
-
IC50 at pH 5.6: 0.0014 mM, IC50 at pH 6.5: 0.0043 mM
Monoiodoacetic acid
-
1 mM, 14% inhibition; 1 mM, 25% inhibition
Monoiodoacetic acid
-
complete inhibition at 1 mM, at 30°C and pH 3.1
Nalpha-tosyl-L-Lys-chloromethyl ketone
-
1 mM, 13% inhibition, isoenzyme MpiCP-2
Nalpha-tosyl-L-Lys-chloromethyl ketone
-
1 mM, 13% inhibition
Nalpha-tosyl-L-Phe-chloromethyl ketone
-
1 mM, 12% inhibition, isoenzyme MpiCP-2
Nalpha-tosyl-L-Phe-chloromethyl ketone
-
1 mM, 57% inhibition
omuralide
-
might inhibit cathepsin A at the S1 subsite in the active-site cleft through direct binding to the active serine residue
omuralide
-
IC50 at pH 5.6: 0.000099 mM, IC50 at pH 6.5: 0.000012 mM
omuralide
-
IC50 at pH 5.6: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
omuralide
-
IC50 at pH 5.6: 0.0000048 mM, IC50 at pH 6.5: 0.000002 mM
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities
PCMB
-
1 mM, 28% inhibition, isoenzyme MpiCP-1; 1 mM, 97% inhibition, isoenzyme MpiCP-2
PCMB
-
1 mM, 95% inhibition
pepstatin A
-
1 mM, 11% inhibition, isoenzyme MpiCP-2; 1 mM, 19% inhibition, isoenzyme MpiCP-1
pepstatin A
-
1 mM, 8% inhibition
Phenylmethylsulfonylfluoride
-
1 mM, 61% inhibition, isoenzyme MpiCP-1; 1 mM, complete inhibition, isoenzyme MpiCP-2
Phenylmethylsulfonylfluoride
-
1 mM, 72% inhibition
Phenylmethylsulfonylfluoride
-
48% residual activity at 1 mM
piperastatin A
-
IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
piperastatin A
-
1 mM, 17% inhibition, isoenzyme MpiCP-2; 1 mM, 87% inhibition, isoenzyme MpiCP-1
piperastatin A
-
1 mM, 70% inhibition
piperastatin A
-
IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 mM
piperastatin A
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
poststatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
poststatin
-
IC50 at pH 5.6: 0.089 mM, IC50 at pH 6.5: 0.029 mM
poststatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
additional information
-
sublethal dose of sortin 1 cause reversible defects in vacuole biogenesis and root development. Treatment with sortin 1 results in carboxypeptidase Y secretion
-
additional information
Citrus sp.
-
not inhibition by EDTA
-
additional information
-
CathA inhibitor affects spermatophore wall digestion
-
additional information
-
not inhibited by trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
additional information
-
no inhibition with 1 mM EDTA or chymostatin
-
additional information
-
20 mM 2-mercaptoethanol strongly inhibits the traffic of phaseolin, causing mainly accumulation in the endoplasmic reticulum or cis-Golgi cisternae, the inhibitory effect is more marked on the vacuolar sorting machinery
-
additional information
-
no inhibition by 1,10-phenanthroline; not inhibition by EDTA
-
additional information
-
in crude extract from baker's yeast carboxypeptidase Y is predominantly found in an inactive form
-
additional information
-
studies on the carboxypeptidase Y-inhibitor complex of yeast
-
additional information
-
not inhibited by ICh, a homolog of carboxypeptidase inhibitor IC
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.363
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine
-
-
0.0082 - 0.21
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
0.0024 - 0.009
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
0.00059 - 0.0025
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
0.0001 - 0.00013
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
0.0001 - 0.00012
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
0.61
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
1.2 - 1.28
acetyl-Phe ethyl ester
0.74
Acetyl-Phe-Leu
-
pH 6.5, 25°C
2.4
Acetyl-Tyr-ethyl ester
0.07
benzoyl-Ala benzyl ester
-
pH 7.5
14
benzoyl-Ala-OGly
-
pH 6.5
6.3
benzoyl-Ala-OMe
-
pH 7.5
1.7
benzoyl-Gly benzyl ester
-
pH 7.5
10
benzoyl-Gly-Arg
-
pH 6.5, 25°C
0.45
benzoyl-Gly-beta-phenyllactate
-
pH 6.0, 25°C
21
benzoyl-Gly-OEt
-
pH 7.5
56
benzoyl-Gly-OGly
-
pH 6.5
48
benzoyl-Gly-OMe
-
pH 7.5
0.05
benzoyl-Gly-OPhe
-
pH 6.5
7.7
benzoyl-Gly-Phe
-
pH 6.5, 25°C
1.1
benzoyl-Phe-Gly
-
pH 6.5
2.4
benzoyl-Phe-OGly
-
pH 6.5
0.18
benzoyl-Phe-OMe
-
pH 7.5
0.13
benzoyl-Tyr-p-nitroanilide
-
-
3.26
Benzyloxycarbonyl-Ala-Ala
-
pH 6.5, 25°C
0.57 - 4.2
Benzyloxycarbonyl-Ala-Phe
4
benzyloxycarbonyl-Arg-Pro
Citrus sp.
-
orange peel
0.053 - 3.3
benzyloxycarbonyl-Glu-Phe
0.14 - 3
Benzyloxycarbonyl-Glu-Tyr
1.15 - 9.09
Benzyloxycarbonyl-Gly-Glu
1.75
benzyloxycarbonyl-Gly-Gly
-
pH 6.5, 25°C
0.83 - 9.1
Benzyloxycarbonyl-Gly-Leu
0.41 - 19
Benzyloxycarbonyl-Gly-Phe
0.1 - 0.38
Benzyloxycarbonyl-His-Phe
0.83 - 1.82
benzyloxycarbonyl-His-Tyr
0.068
benzyloxycarbonyl-Leu-Leu
-
pH 6.5, 25°C
0.1 - 0.5
benzyloxycarbonyl-Leu-Phe
0.56
benzyloxycarbonyl-Phe-Ala
-
pH 6.5, 25°C
9
benzyloxycarbonyl-Phe-beta-Ala
-
pH 6.5, 25°C
0.36 - 16.5
benzyloxycarbonyl-Phe-Glu
4
benzyloxycarbonyl-Phe-Gly
0.9 - 3.2
benzyloxycarbonyl-Phe-His
0.07 - 3
Benzyloxycarbonyl-Phe-Leu
10 - 15
benzyloxycarbonyl-Phe-NH2
0.67
benzyloxycarbonyl-Phe-Pro
-
pH 6.5, 25°C
0.86 - 1.55
benzyloxycarbonyl-Tyr-Glu
0.04
CBZ-Phe-Leu
recombinant protein, pH 4.5, 27°C
0.075
Furylacryloyl-Phe ethyl ester
-
wild-type
0.14
furylacryloyl-Phe-Ala
-
pH 6.5
5.4
furylacryloyl-Phe-Gly
-
pH 6.5
0.021
furylacryloyl-Phe-Leu
-
pH 6.5
0.16
Furylacryloyl-Phe-OGly-OH
-
wild-type
0.39
furylacryloyl-Phe-OMe
-
pH 7.5
0.047
furylacryloyl-Phe-Val
-
pH 6.5
0.45
Hippuryl-beta-phenyl lactate
-
-
0.029
N-benzoyl-L-tyrosine-p-nitroanilide
-
-
additional information
additional information
-
0.0082
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
0.024
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
0.035
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
0.21
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
0.0024
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 5.0
0.009
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 6.5
0.00059
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
0.0025
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
0.0001
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
0.00013
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
0.0001
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
0.00012
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
1.2
acetyl-Phe ethyl ester
-
pH 8.0, 25°C
1.28
acetyl-Phe ethyl ester
-
pH 6.5, 25°C
2.4
Acetyl-Tyr-ethyl ester
-
-
2.4
Acetyl-Tyr-ethyl ester
-
pH 8.0, 25°C
0.57
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341G
0.98
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341F
1.1
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, wild-type enzyme anf mutant enzyme C341V
4.2
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341S
0.053
benzyloxycarbonyl-Glu-Phe
-
pH 6.5, 25°C
0.13
benzyloxycarbonyl-Glu-Phe
-
pH 5.5, 25°C
3.3
benzyloxycarbonyl-Glu-Phe
-
pH 6.5, 25°C
0.14
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.0, 25°C
0.5
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.5, 25°C
3
Benzyloxycarbonyl-Glu-Tyr
-
pH 6.0, 25°C
1.15
Benzyloxycarbonyl-Gly-Glu
-
pH 4.5, 25°C
9.09
Benzyloxycarbonyl-Gly-Glu
-
pH 5.5, 25°C
0.83
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, wild-type enzyme
0.89
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341V
3.2
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341G
5.2
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341S
8.4
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341F
9.1
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341D
0.41
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, wild-type enzyme
0.45
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341V
1.7
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C
3.7
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341G
6.7
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341S
19
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341F
0.1
Benzyloxycarbonyl-His-Phe
-
pH 6.5, 25°C
0.23
Benzyloxycarbonyl-His-Phe
-
pH 7.0, 25°C
0.38
Benzyloxycarbonyl-His-Phe
-
pH 7.5, 25°C
0.83
benzyloxycarbonyl-His-Tyr
-
pH 5.7, 25°C
1.33
benzyloxycarbonyl-His-Tyr
-
pH 6.5, 25°C
1.82
benzyloxycarbonyl-His-Tyr
-
pH 7.5, 25°C
0.1
benzyloxycarbonyl-Leu-Phe
-
pH 6.5, 25°C
0.5
benzyloxycarbonyl-Leu-Phe
-
pH 6.5, 25°C
0.5
benzyloxycarbonyl-Leu-Phe
-
benzyloxycarbonyl-Phe-Phe at pH 6.5
0.5
benzyloxycarbonyl-Leu-Phe
Citrus sp.
-
orange peel
0.36
benzyloxycarbonyl-Phe-Glu
-
pH 4.5, 25°C
0.41
benzyloxycarbonyl-Phe-Glu
-
pH 5.5, 25°C
0.41
benzyloxycarbonyl-Phe-Glu
-
furylacryloyl-Phe-Gly-OH
16.5
benzyloxycarbonyl-Phe-Glu
-
pH 6.5, 25°C
4
benzyloxycarbonyl-Phe-Gly
-
pH 6.5
4
benzyloxycarbonyl-Phe-Gly
-
pH 6.5, 25°C
0.9
benzyloxycarbonyl-Phe-His
-
pH 5.5, 25°C
3.2
benzyloxycarbonyl-Phe-His
-
pH 6.5, 25°C
0.07
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341F
0.1
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C
0.16
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341V
0.19
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, wild-type enzyme
0.24
Benzyloxycarbonyl-Phe-Leu
-
pH 6.0, 25°C
0.26
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341G
0.32
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341S
3
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341D
10
benzyloxycarbonyl-Phe-NH2
-
pH 8.0
10
benzyloxycarbonyl-Phe-NH2
-
pH 8.0, 25°C
11
benzyloxycarbonyl-Phe-NH2
-
pH 7.0, 25°C
15
benzyloxycarbonyl-Phe-NH2
-
pH 6.0, 25°C
0.86
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37°C
1.33
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37°C, isoenzyme MpiCP-1
1.55
benzyloxycarbonyl-Tyr-Glu
-
pH 3.5, 37°C, isoenzyme MpiCP-2
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic characterization of peptide semisynthesis
-
additional information
additional information
-
overview: synthetic substrates
-
additional information
additional information
-
influence of mercurials
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
237
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine
-
-
2.7 - 6.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
2.2 - 3.8
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
2.5 - 3.9
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
2.3 - 3.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
2.3 - 3.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
1777
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
120 - 122
acetyl-Phe ethyl ester
36.1
Acetyl-Phe-Leu
-
pH 6.5, 25°C
105
Acetyl-Tyr ethyl ester
123
benzoyl-Ala benzyl ester
-
pH 7.5
58.3
benzoyl-Ala-OGly
-
pH 6.5
51.7
benzoyl-Ala-OMe
-
pH 7.5
18.3
benzoyl-Gly benzyl ester
-
pH 7.5
1.44
benzoyl-Gly-Arg
-
pH 6.5, 25°C
21.2
benzoyl-Gly-beta-phenyllactate
-
pH 6.0, 25°C
2.5
benzoyl-Gly-OEt
-
pH 7.5
30
benzoyl-Gly-OGly
-
pH 6.5
2.5
benzoyl-Gly-OMe
-
pH 7.5
18.3
benzoyl-Gly-OPhe
-
pH 6.5
3.8 - 3.83
benzoyl-Gly-Phe
11.5
benzoyl-Phe-Gly
-
pH 6.5
35
benzoyl-Phe-OGly
-
pH 6.5
152
benzoyl-Phe-OMe
-
pH 7.5
2.1
benzoyl-Tyr-4-nitroanilide
-
-
69.4
Benzyloxycarbonyl-Ala-Ala
-
pH 6.5, 25°C
465
Benzyloxycarbonyl-Ala-Leu
-
-
2.2 - 150
Benzyloxycarbonyl-Ala-Phe
13.3 - 16.8
benzyloxycarbonyl-Glu-Phe
18.8 - 23.8
Benzyloxycarbonyl-Glu-Tyr
0.32 - 0.46
Benzyloxycarbonyl-Gly-Glu
2.18
benzyloxycarbonyl-Gly-Gly
-
pH 6.5, 25°C
0.467 - 7
Benzyloxycarbonyl-Gly-Leu
0.16 - 5.5
Benzyloxycarbonyl-Gly-Phe
0.72 - 2.05
Benzyloxycarbonyl-His-Phe
8.2 - 10.7
benzyloxycarbonyl-His-Tyr
6.85
benzyloxycarbonyl-Leu-Leu
-
pH 6.5, 25°C
46
benzyloxycarbonyl-Leu-Phe
-
pH 6.5, 25°C
120
benzyloxycarbonyl-Phe-Ala
-
pH 6.5, 25°C
66
benzyloxycarbonyl-Phe-beta-Ala
-
pH 6.5, 25°C
24.5 - 96.5
benzyloxycarbonyl-Phe-Glu
140
benzyloxycarbonyl-Phe-Gly
3 - 11.6
benzyloxycarbonyl-Phe-His
1.2 - 130
Benzyloxycarbonyl-Phe-Leu
2.2 - 5.33
benzyloxycarbonyl-Phe-NH2
420
benzyloxycarbonyl-Phe-Phe
23
benzyloxycarbonyl-Phe-Pro
-
pH 6.5, 25°C
291 - 2039
benzyloxycarbonyl-Tyr-Glu
12.1
CBZ-Phe-Leu
recombinant protein, pH 4.5, 27°C
68.3
Furylacryloyl-Phe ethyl ester
-
wild-type enzyme
162
furylacryloyl-Phe-Ala
-
pH 6.5
96.7
furylacryloyl-Phe-Gly
-
pH 6.5
81.7
furylacryloyl-Phe-Leu
-
pH 6.5
24.2 - 61.7
Furylacryloyl-Phe-OGly-OH
183
furylacryloyl-Phe-OMe
-
pH 7.5
108
furylacryloyl-Phe-Val
-
pH 6.5
21.2
Hippuryl-beta-phenyl lactate
-
-
additional information
additional information
-
2.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
4.1
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
5.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
6.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
2.2
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 6.5
3.8
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 5.0
2.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
3.9
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
2.3
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
3.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
2.3
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
3.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
120
acetyl-Phe ethyl ester
-
pH 8.0, 25°C
122
acetyl-Phe ethyl ester
-
pH 6.5, 25°C
105
Acetyl-Tyr ethyl ester
-
-
105
Acetyl-Tyr ethyl ester
-
pH 8.0, 25°C
3.8
benzoyl-Gly-Phe
-
pH 6.5, 25°C
3.83
benzoyl-Gly-Phe
-
pH 6.5
2.2
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341F
8
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341V
93
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341S
95
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, mutant enzyme C341G
150
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, wild-type enzyme
13.3
benzyloxycarbonyl-Glu-Phe
-
pH 6.5, 25°C
15.5
benzyloxycarbonyl-Glu-Phe
-
pH 4.5, 25°C
16.8
benzyloxycarbonyl-Glu-Phe
-
pH 5.5, 25°C
18.8
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.0, 25°C
19
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.5, 25°C
23.8
Benzyloxycarbonyl-Glu-Tyr
-
pH 6.0, 25°C
0.32
Benzyloxycarbonyl-Gly-Glu
-
pH 4.5, 25°C
0.46
Benzyloxycarbonyl-Gly-Glu
-
pH 5.5, 25°C
0.467
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341V
1.4
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341D
1.9
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341S
2.3
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341F
3.2
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, wild-type enzyme
7
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25°C, mutant enzyme C341G
0.16
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341V
0.96
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, wild-type enzyme
1.1
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341G
2.2
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C
2.4
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341S
5.5
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25°C, mutant enzyme C341F
0.72
Benzyloxycarbonyl-His-Phe
-
pH 6.5, 25°C
1.82
Benzyloxycarbonyl-His-Phe
-
pH 7.0, 25°C
2.05
Benzyloxycarbonyl-His-Phe
-
pH 7.5, 25°C
8.2
benzyloxycarbonyl-His-Tyr
-
pH 6.5 or pH 7.5, 25°C
10.7
benzyloxycarbonyl-His-Tyr
-
pH 5.7, 25°C
24.5
benzyloxycarbonyl-Phe-Glu
-
pH 4.5, 25°C
26.2
benzyloxycarbonyl-Phe-Glu
-
pH 5.5, 25°C
96.5
benzyloxycarbonyl-Phe-Glu
-
pH 6.5, 25°C
140
benzyloxycarbonyl-Phe-Gly
-
-
140
benzyloxycarbonyl-Phe-Gly
-
pH 6.5, 25°C
3
benzyloxycarbonyl-Phe-His
-
pH 5.5, 25°C
11.6
benzyloxycarbonyl-Phe-His
-
pH 6.5, 25°C
1.2
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341F
2.1
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341D
4.6
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341V
15
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341G
15.1
Benzyloxycarbonyl-Phe-Leu
-
pH 6.0
18
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, mutant enzyme C341S
92
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C, wild-type enzyme
130
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25°C
2.2
benzyloxycarbonyl-Phe-NH2
-
pH 7.0, 25°C
2.8
benzyloxycarbonyl-Phe-NH2
-
pH 6.0, 25°C
5.3
benzyloxycarbonyl-Phe-NH2
-
pH 8.0, 25°C
5.33
benzyloxycarbonyl-Phe-NH2
-
pH 8.0
420
benzyloxycarbonyl-Phe-Phe
-
-
420
benzyloxycarbonyl-Phe-Phe
-
pH 6.5, 25°C
291
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37°C
723
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37°C, isoenzyme MpiCP-1
2039
benzyloxycarbonyl-Tyr-Glu
-
pH 3.5, 37°C, isoenzyme MpiCP-2
24.2
Furylacryloyl-Phe-OGly-OH
-
wild-type enzyme
61.7
Furylacryloyl-Phe-OGly-OH
-
wild-type enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
conformational differences reflected in kinetic behaviour in water and deuterium oxide
-
additional information
additional information
-
influence of mercurials
-
additional information
additional information
-
overview: synthetic substrates
-
additional information
additional information
-
kinetic characterization of peptide semisynthesis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0078
(3R)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000057
(3S)-3-(([1-(2-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000357
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methoxyphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000038
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000252
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(3-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000274
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000375
(3S)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-[2-(trifluoromethyl)phenyl]propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0001
(3S)-3-(([1-(3-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000059
(3S)-3-(([1-(3-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000087
(3S)-3-(([1-(4-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00011
(3S)-3-(([4-chloro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00003
(3S)-3-(([4-fluoro-1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00006
(3S)-3-(2,4-dichlorophenyl)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000005 - 0.00005
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
0.00007
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00011
(3S)-3-([(4-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0001
(3S)-3-([(4-methoxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00007
(3S)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000003
(3S)-3-([[5-(3,3-dimethyl-2-oxobutoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000015
(3S)-3-([[5-(cyclopropylmethoxy)-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000015
(3S)-3-([[5-ethoxy-1-(2-fluorophenyl)-1H-pyrazol-3-yl]carbonyl]amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00001
(3S)-3-[([1-(2-fluorophenyl)-5-[(2S)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0006
3,4-dichloroisocoumarin
Homo sapiens
-
-
0.00538
3-(([1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(4-fluorophenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000226
3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-phenylpropanoic acid
Homo sapiens
-
pH 6, 37°C
0.000026
3-(([1-(2-fluorophenyl)-5-methoxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2-methylphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.03
3-(([1-(4-chlorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)-3-(2,5-dichlorophenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00012
3-(2,3-dichlorophenyl)-3-(([1-(2,4-difluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0001
3-(2,3-dichlorophenyl)-3-([(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000025
3-(4'-fluorobiphenyl-4-yl)-3-([[1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000076
3-(5-fluoro-2-methylphenyl)-3-(([1-(2-fluorophenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl)amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.000803
3-(biphenyl-4-yl)-3-([[1-(2,5-dimethylphenyl)-5-hydroxy-1H-pyrazol-3-yl]carbonyl]amino)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0002
3-[[(5-hydroxy-1-phenyl-1H-pyrazol-3-yl)carbonyl]amino]-3-(4-phenoxyphenyl)propanoic acid
Homo sapiens
-
pH 6, 37°C
0.01
diisopropyl fluorophosphate
Homo sapiens
-
-
0.00002 - 0.002
ebelactone B
0.0014 - 0.048
lactacystin
0.000002 - 0.000099
omuralide
0.72
Phe-Asn-Arg-Ala-Val-Asp
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.63
Phe-Asn-Arg-Ala-Val-Val
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.91
Phe-Asn-Arg-Pro-Val-Asp
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.71
Phe-Asn-Arg-Pro-Val-Val
Homo sapiens
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.0041 - 0.1
piperastatin A
0.000005
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
Homo sapiens
-
pH 6, 37°C
0.00005
(3S)-3-(2,4-dichlorophenyl)-3-[([1-(2-fluorophenyl)-5-[(2R)-2-hydroxy-3,3-dimethylbutoxy]-1H-pyrazol-3-yl]carbonyl)amino]propanoic acid
Homo sapiens
-
pH 6, 37°C
0.0022 - 0.013
chymostatin
Triticum aestivum
-
IC50 at pH 5.6: 0.013 mM, IC50 at pH 6.5: 0.0022 mM
0.092 - 0.1
chymostatin
Homo sapiens
-
IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
0.1
chymostatin
Saccharomyces cerevisiae
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
0.00002 - 0.00003
ebelactone B
Saccharomyces cerevisiae
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
0.0015
ebelactone B
Triticum aestivum
-
IC50: 0.0021 mM (at pH 5.6), IC50: 0.0015 mM (at pH 6.5)
0.0016 - 0.002
ebelactone B
Homo sapiens
-
IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
0.0014 - 0.0043
lactacystin
Triticum aestivum
-
IC50 at pH 5.6: 0.0014 mM, IC50 at pH 6.5: 0.0043 mM
0.0018 - 0.0052
lactacystin
Homo sapiens
-
IC50 at pH 5.6: 0.0052 mM, IC50 at pH 6.5: 0.0018 mM
0.031 - 0.048
lactacystin
Saccharomyces cerevisiae
-
IC50 at pH 5.6: 0.048 mM, IC50 at pH 6.5: 0.031 mM
0.000002 - 0.0000048
omuralide
Triticum aestivum
-
IC50 at pH 5.6: mM, IC50 at pH 6.5: 0.000002 mM
0.000012 - 0.000099
omuralide
Homo sapiens
-
IC50 at pH 5.6: 0.000099 mM, IC50 at pH 6.5: 0.000012 mM
0.000078 - 0.000096
omuralide
Saccharomyces cerevisiae
-
IC50 at pH 5.6: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
0.0041 - 0.0045
piperastatin A
Saccharomyces cerevisiae
-
IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 mM
0.018 - 0.032
piperastatin A
Homo sapiens
-
IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
0.1
piperastatin A
Triticum aestivum
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
0.029 - 0.089
poststatin
Saccharomyces cerevisiae
-
IC50 at pH 5.6:0.089 mM, IC50 at pH 6.5: 0.029 mM
0.1
poststatin
Homo sapiens
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
0.1
poststatin
Triticum aestivum
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
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A251E
the mutant shows increased activity compared to the wild type cathepsin A
K355Q
the mutant shows increased activity compared to the wild type cathepsin A
L354D
the mutant shows decreased activity compared to the wild type cathepsin A
P451A
the mutant shows increased activity compared to the wild type cathepsin A
R20A
the mutant shows decreased activity compared to the wild type cathepsin A
R262A/R292A
double mutant also undergoes processing to form large and small subunits, suggesting alternative avenues for the maturation of cathepsin A
R344A
the mutant shows about wild type cathepsin A activity
R344D
inactive mutant, the 54 kDa precursor/zymogen with the R344D substitution is not processed to the 32/20 kDa mature form with CathA activity
R344E
the mutant shows reduced cathepsin A activity compared to the wild type
R344G
the mutant shows reduced cathepsin A activity compared to the wild type
R344I
the mutant shows reduced cathepsin A activity compared to the wild type
R344K
the mutant shows reduced cathepsin A activity compared to the wild type
R344M
the mutant shows reduced cathepsin A activity compared to the wild type
R344N
the mutant shows reduced cathepsin A activity compared to the wild type
R344P
the mutant shows reduced cathepsin A activity compared to the wild type
R344Q
the mutant shows reduced cathepsin A activity compared to the wild type
R344S
the mutant shows about wild type cathepsin A activity
R344V
the mutant shows reduced cathepsin A activity compared to the wild type
S150A/R284A/R298A
triple mutant S150A/R284A/R298A also undergoes cleavage into large and small subunits, comparable with the wildtype cathepsin A, suggesting that these sites are not mandatory for the activation of cathepsin A
W382A
the mutant shows decreased activity compared to the wild type cathepsin A
T343F
-
the mutant accumulates in the microsomal fraction of protoplasts treated with 2-mercaptoethanol and is for the most part susceptible to digestion by endoglycosidase H
C341F
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
C341G
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu and benzyloxycarbonyl-Gly-Phe, somewhat increased ratio with benzyloxycarbonyl-Ala-Phe
C341S
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
C341V
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
E355Q
-
mutant shows moderate CPY secretion
E365A
-
mutant shows moderate CPY secretion
E369A
-
mutant shows moderate CPY secretion
E371A
-
mutant shows CPY secretion similar to the wild type
G255R
-
PNGase releases N-glycans from the mutant during the endoplasmic reticulum-associated degradation process in vivo. A major endoproteolytic reaction on the mutant appears to occur between amino acid 400 and 404
L267A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 18.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 113% for furylacryloyl-Ala-Lys, 130% for furylacryloyl-Ala-Arg,10.8% for furylacryloyl-Phe-Ala, 18.5% for furylacryloyl-Phe-Val and 31.3% for furylacryloyl-Phe-Leu
L267D
-
mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1'
L267D/L272D
-
mutant enzyme with a preference for substrates with C-terminal basic amino acid residues
L267E
-
mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1'
L267F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 88.5% for furylacryloyl-Ala-Leu, 65.2% for furylacryloyl-Ala-Glu, 44% for furylacryloyl-Ala-Lys, 53% for furylacryloyl-Ala-Arg, 34.2% for furylacryloyl-Phe-Ala, 57.8% for furylacryloyl-Phe-Val and 82.6% for furylacryloyl-Phe-Leu
L267K
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L267Q
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 17% for furylacryloyl-Ala-Leu, 48% for furylacryloyl-Ala-Glu, 157% for furylacryloyl-Ala-Lys, 63% for furylacryloyl-Ala-Arg
L267R
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L272A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 8.7% for furylacryloyl-Ala-Leu, 60.9% for furylacryloyl-Ala-Glu, 127% for furylacryloyl-Ala-Lys, 47% for furylacryloyl-Ala-Arg, 78.9% for furylacryloyl-Phe-Ala, 50% for furylacryloyl-Phe-Val and 15.6% for furylacryloyl-Phe-Leu
L272F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 83% for furylacryloyl-Ala-Leu, 95.7% for furylacryloyl-Ala-Glu, 46% for furylacryloyl-Ala-Lys, 63% for furylacryloyl-Ala-Arg, 113% for furylacryloyl-Phe-Ala, 121% for furylacryloyl-Phe-Val and 83.4% for furylacryloyl-Phe-Leu
L272K
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
L272R
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
N356A
-
mutant shows CPY secretion similar to the wild type
N87I
-
mutant enzyme with reduced transport rate and reduced enzymatic activity, 30%
S297A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 39.7% for furylacryloyl-Ala-Leu, 161% for furylacryloyl-Ala-Glu, 66% for furylacryloyl-Ala-Lys, 80% for furylacryloyl-Ala-Arg, 126% for furylacryloyl-Phe-Ala, 109% for furylacryloyl-Phe-Val and 88.6% for furylacryloyl-Phe-Leu
S297F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 43.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 42% for furylacryloyl-Ala-Lys, 6.7% for furylacryloyl-Ala-Arg, 86.8% for furylacryloyl-Phe-Ala, 55% for furylacryloyl-Phe-Val and 60.9% for furylacryloyl-Phe-Leu
S297K
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
S297R
-
mutation does not increase the rather low activity towards substrates with Glu in the P1' position but greatly reduces the activity towards substrates with C-terminal Lys or Arg due to electrostatic repulsion
nutrition
-
the enzyme can be used to eliminate the bitterness of bitter peptides
L267D/L272A
-
-
L267D/L272A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 1.2% for furylacryloyl-Ala-Leu, 13% for furylacryloyl-Ala-Glu, 423% for furylacryloyl-Ala-Lys, 70% for furylacryloyl-Ala-Arg
L272D
-
-
L272D
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 10.4% for furylacryloyl-Ala-Leu, 67% for furylacryloyl-Ala-Glu, 61.9% for furylacryloyl-Ala-Lys, 26% for furylacryloyl-Ala-Arg
L272E
-
-
L272E
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 4% for furylacryloyl-Ala-Leu, 30% for furylacryloyl-Ala-Glu, 257% for furylacryloyl-Ala-Lys, 70% for furylacryloyl-Ala-Arg
L272Q
-
-
L272Q
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 3.3% for furylacryloyl-Ala-Leu, 70% for furylacryloyl-Ala-Glu, 87% for furylacryloyl-Ala-Lys, 32% for furylacryloyl-Ala-Arg
L272R/M398F
-
-
L272R/M398F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 6.3% for furylacryloyl-Ala-Leu, 176% for furylacryloyl-Ala-Glu, 0.3% for furylacryloyl-Ala-Lys, 0.2% for furylacryloyl-Ala-Arg
L272R/T60F
-
-
L272R/T60F
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 60% for furylacryloyl-Ala-Leu, 172% for furylacryloyl-Ala-Glu, 2.8% for furylacryloyl-Ala-Lys, 2.1% for furylacryloyl-Ala-Arg
S297D
-
-
S297D
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 39.6% for furylacryloyl-Ala-Leu, 72% for furylacryloyl-Ala-Glu, 73% for furylacryloyl-Ala-Lys, 25% for furylacryloyl-Ala-Arg
S297E
-
-
S297E
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 27% for furylacryloyl-Ala-Leu, 63% for furylacryloyl-Ala-Glu, 58% for furylacryloyl-Ala-Lys, 24% for furylacryloyl-Ala-Arg
S297Q
-
-
S297Q
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 25% for furylacryloyl-Ala-Leu, 80% for furylacryloyl-Ala-Glu, 41% for furylacryloyl-Ala-Lys, 19.3% for furylacryloyl-Ala-Arg
T60F/L267D/L272A
-
-
T60F/L267D/L272A
-
kcat/Km of mutant enzyme in% of the of the wildtype value: 6% for furylacryloyl-Ala-Leu, 80% for furylacryloyl-Ala-Glu, 789% for furylacryloyl-Ala-Lys, 280% for furylacryloyl-Ala-Arg
additional information
-
the gene vps4 null mutant missorts the vacuolar enzyme carboxypeptidase Y
additional information
a yeast two-hybrid screening using a cDNA library of osteoclast precursors discloses PPCA as a binding partner of NF-kappaB p50/p65. Forced expression of PPCA with p50/p65 in HEK293 cells decreases both the level of p50/p65 proteins and the transcriptional activity. Overexpression of PPCA causes the disappearance of p50/p65 in both the lysosomal and cytosolic fractions. PPCA is expressed throughout osteoclastogenesis,and the expression is slightly up-regulated by nuclear factor (NF)-kappaB ligand signaling. Knockdown of PPCA in osteoclast precursors with PPCA siRNA stimulates binding of nuclear proteins to oligonucleotides containing an NF-kappaB binding motif and increases osteoclastogenesis
additional information
-
carboxypeptidase Y is partially missorted to the cell surface in certain mutants of the COPIB subcomplex (COPIb, Sec27, Sec28, and possibly Sec33), which indicates an impairment in endosomal transport
additional information
-
the gene vps4 null mutant missorts the vacuolar enzyme carboxypeptidase Y
additional information
-
three signal sequences of Saccharomyces cerevisiae mating factor a (MFalpha) and invertase (SUC2), and Kluyveromyces marxianus inulinase (INU1) are combined with proCPY to increase a transporting efficiency from the endoplasmic reticulum in Saccharomyces cerevisiae. The MFalpha signal sequence gives the best specific activity of extracellular CPY
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