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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
-
-
?