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Information on EC 3.4.16.5 - carboxypeptidase C
for references in articles please use BRENDA:EC3.4.16.5
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.16 Serine-type carboxypeptidases
3.4.16.5 carboxypeptidase C
IUBMB Comments
A carboxypeptidase with optimum pH 4.5–6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in ). Widely distributed in eukaryotes. Type example of peptidase family S10.
The enzyme appears in viruses and cellular organisms
- 3.4.16.5
- vacuolar
- edulis
- proteinase
-
galactosialidosis
- beta-galactosidase
-
cathinone
- invertase
- aminopeptidase
- neuraminidase
-
edman
-
deamidation
-
missorting
-
chew
-
endosome
-
cyanogen
- amphetamine
- sialidase
-
prevacuolar
-
forsk
- alpha-factor
-
mislocalization
- sialidosis
-
psychoactive
-
psychostimulant
-
transpeptidation
-
er-associated
- prolylcarboxypeptidase
-
exopeptidase
-
amphetamine-like
-
post-golgi
-
lysosome-like
-
intralysosomal
- prc1
-
procarboxypeptidase
- celastraceae
-
peninsula
- analysis
- synthesis
- nutrition
- molecular biology
showSynonyms
carboxypeptidase y, cathepsin a, catha, deamidase, serine carboxypeptidase, protective protein/cathepsin a, scpep1, procpy, carboxypeptidase yscy, carboxypeptidase-y, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATG42
carboxypeptidase a
carboxypeptidase C
carboxypeptidase Y
carboxypeptidase YSCY
-
-
-
-
CatA
CathA
cathepsin A
CP-MI
-
-
-
-
CP-MIII
-
-
-
-
CP-WIII
-
-
-
-
CPC
CPY
CTSA
deamidase
-
-
-
-
EC 3.4.12.1
-
-
formerly
-
EC 3.4.16.3
-
-
formerly
-
lysosomal carboxypeptidase A
lysosomal protective protein
MO54
-
-
-
-
Phaseolin
PpcA
PRC1
protective protein/cathepsin A
Scpep1
Ser carboxypeptidase-like protein
-
SCPL, SCPL proteins bear the trademark Ser-Asp-His catalytic triad along with other sequence features that are characteristic of known Ser carboxypeptidases
serine carboxypeptidase
serine carboxypeptidase I
TcCBP
vacuolar serine carboxypeptidase Y
Ybr139w
additional information
carboxypeptidase Y
-
-
-
-
carboxypeptidase Y
-
-
cathepsin A
-
-
-
-
CPY
-
-
-
-
CPY
-
-
lysosomal carboxypeptidase A
-
-
-
-
lysosomal protective protein
-
-
-
-
Phaseolin
-
-
-
-
serine carboxypeptidase I
-
-
-
-
additional information
-
this enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC 3.4.16.3, not a homologue of chymotrypsin or subtilisin, see reference
additional information
-
this enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC 3.4.16.3, not a homologue of chymotrypsin or subtilisin, see reference
additional information
-
this enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC 3.4.16.3, not a homologue of chymotrypsin or subtilisin, see reference
additional information
-
this enzyme is probably also identical to lysosomal tyrosine carboxypeptidase, formerly EC 3.4.16.3, not a homologue of chymotrypsin or subtilisin, see reference
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of a C-terminal amino acid with broad specificity
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9046-67-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(L-Ala)5 + H2O
(L-Ala)4 + L-Ala
Substrates: 100% hydrolysis
Products: -
Products: -
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5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu-Arg + H2O
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu + Arg
-
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-(L-Ala)5 + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-(L-Ala)4 + L-Ala
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-Gly-Gly-L-His + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-Gly-Gly + L-His
Substrates: 30% hydrolysis at pH 6.8, 15% hydrolysis at pH 5.5
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-Gly-L-Tyr + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-Gly + L-Tyr
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Ala-Gly-Gly + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Ala-Gly + Gly
Substrates: 100% hydrolysis at pH 5.5
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Ala-L-Leu + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Ala + L-Leu
Substrates: 100% hydrolysis
Products: -
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?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Arg-Gly-L-Asp + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Arg-Gly + L-Asp
Substrates: 100% hydrolysis
Products: -
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?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Asp-L-Asp + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Asp + L-Asp
Substrates: 100% hydrolysis at pH 4.5, 85% hydrolysis at pH 5.5, 15% hydrolysis at pH 6.8
Products: -
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?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Leu-L-Leu + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Leu + L-Leu
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Lys-L-Tyr-L-Lys + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Lys-L-Tyr + L-Lys
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Phe-L-Ala + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Phe + L-Ala
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Thr-L-Val-L-Leu + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Thr-L-Val + L-Leu
Substrates: 100% hydrolysis
Products: -
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?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Asp + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Asp
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Glu + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Glu
Substrates: -
Products: -
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?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Leu + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Leu
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Lys + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Lys
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Phe + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Phe
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Pro + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Pro
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Tyr + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Tyr
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe-L-Val + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Tyr-Gly-L-Leu-L-Phe + L-Val
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val-L-Met + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val + L-Met
Substrates: 100% hydrolysis
Products: -
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?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val-L-Pro + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val + L-Pro
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val-L-Ser + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val + L-Ser
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val-L-Tyr + H2O
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-L-Val + L-Tyr
Substrates: 100% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccinimidyl carbamoyl-L-Tyr-L-Ala-Gly-L-Phe-L-Leu + H2O
6-aminoquinoline-N-hydroxysuccinimidyl carbamoyl-L-Tyr-L-Ala-Gly-L-Phe + L-Leu
Substrates: -
Products: -
Products: -
?
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine + H2O
?
-
Substrates: -
Products: -
Products: -
?
9-fluorenylmethoxycarbonyl-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu + Ala
-
Substrates: -
Products: -
Products: -
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu + Ala
-
Substrates: -
Products: -
Products: -
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu + Ala
-
Substrates: -
Products: -
Products: -
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu + Ala
-
Substrates: -
Products: -
Products: -
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu + Ala
-
Substrates: -
Products: -
Products: -
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu + Ala
-
Substrates: -
Products: -
Products: -
?
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe ethyl ester + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-Phe-Leu + H2O
acetyl-Phe + Leu
-
Substrates: -
Products: -
Products: -
?
acetyl-Tyr-ethyl ester + H2O
?
-
Substrates: -
Products: -
Products: -
?
adrenocorticotropic hormone fragment 7-38 + H2O
?
-
Substrates: -
Products: -
Products: -
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
benzoyl-Gly-Phe + H2O
benzoyl-Gly + Phe
-
Substrates: -
Products: -
Products: -
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
benzoyl-L-tyrosine-p-nitroanilide + H2O
benzoyl-L-tyrosine + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
benzoyl-Phe-Gly + H2O
benzoyl-Phe + Gly
-
Substrates: -
Products: -
Products: -
?
benzoyl-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Ala + H2O
benzyloxycarbonyl-Ala + Ala
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Ala-Leu + H2O
Benzyloxycarbonyl-Ala + Leu
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Arg-Pro + H2O
benzyloxycarbonyl-Arg + Pro
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Leu + H2O
benzyloxycarbonyl-Glu + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Arg + H2O
benzyloxycarbonyl-Gly + Arg
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Glu + H2O
benzyloxycarbonyl-Gly + Glu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
benzyloxycarbonyl-Gly-Gly + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Met + H2O
benzyloxycarbonyl-Gly + Met
-
Substrates: 19% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Pro + H2O
benzyloxycarbonyl-Gly + Pro
-
Substrates: -
Products: -
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?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
benzyloxycarbonyl-Gly-Pro-Leu-Gly + Pro
-
Substrates: 3% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
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?
Benzyloxycarbonyl-Gly-Val + H2O
Benzyloxycarbonyl-Gly + Val
-
Substrates: 24% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-His-Leu + H2O
benzyloxycarbonyl-His + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-His-Phe + H2O
benzyloxycarbonyl-His + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-His-Tyr + H2O
benzyloxycarbonyl-His + Tyr
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Ile-Leu + H2O
benzyloxycarbonyl-Ile + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-L-Phe-L-Leu + H2O
benzyloxycarbonyl-L-Phe + L-Leu
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-L-phenylalanyl-L-leucine + H2O
benzyloxycarbonyl-Phe + Leu
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Leu + H2O
benzyloxycarbonyl-Leu + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Nle-Leu + H2O
benzyloxycarbonyl-Nle + Leu
-
Substrates: -
Products: -
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?
benzyloxycarbonyl-Phe-beta-Ala + H2O
benzyloxycarbonyl-Phe + beta-Ala
-
Substrates: -
Products: -
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?
benzyloxycarbonyl-Phe-Glu + H2O
benzyloxycarbonyl-Phe + Glu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-His + H2O
benzyloxycarbonyl-Phe + His
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-NH2 + H2O
?
-
Substrates: -
Products: -
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?
benzyloxycarbonyl-Phe-Phe + H2O
benzyloxycarbonyl-Phe + Phe
-
Substrates: -
Products: -
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?
benzyloxycarbonyl-Phe-Tyr-Gly + H2O
benzyloxycarbonyl-Phe-Tyr + Gly
-
Substrates: 172% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Tyr-Leu + H2O
benzyloxycarbonyl-Phe-Tyr + Leu
-
Substrates: 120% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Pro-Leu + H2O
benzyloxycarbonyl-Pro + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Pro-Leu + Gly
-
Substrates: isoenzyme MpiCP-2
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?
benzyloxycarbonyl-Ser-Leu + H2O
benzyloxycarbonyl-Ser + Leu
-
Substrates: -
Products: -
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?
benzyloxycarbonyl-Tyr-Gly + H2O
benzyloxycarbonyl-Tyr + Gly
-
Substrates: 188% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
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?
benzyloxycarbonyl-Tyr-Phe + H2O
benzyloxycarbonyl-Tyr + Phe
-
Substrates: 201% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
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?
benzyloxycarbonyl-Val-Leu + H2O
benzyloxycarbonyl-Val + Leu
-
Substrates: -
Products: -
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?
CBZ-Phe-Leu + H2O
N-benzyloxycarbonyl-L-Phe + L-leucine
Substrates: -
Products: -
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?
corticotropin-releasing factor fragment 6-33 + H2O
?
-
Substrates: -
Products: -
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?
furylacryloyl-Ala-Glu + H2O
furylacryloyl-Ala + Glu
-
Substrates: -
Products: -
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?
furylacryloyl-Ala-Leu + H2O
furylacryloyl-Ala + Leu
-
Substrates: -
Products: -
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?
furylacryloyl-Arg-Leu + H2O
furylacryloyl-Arg + Leu
-
Substrates: preferred substrate
Products: -
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?
furylacryloyl-Lys-Ala + H2O
furylacryloyl-Lys + Ala
-
Substrates: -
Products: -
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?
furylacryloyl-Lys-Leu + H2O
furylacryloyl-Lys + leu
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Phe ethyl ester + H2O
?
-
Substrates: -
Products: -
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?
furylacryloyl-Phe-Leu + H2O
furylacryloyl-Phe + Leu
-
Substrates: -
Products: -
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?
furylacryloyl-Phe-Phe + H2O
furylacryloyl-Phe + Phe
-
Substrates: -
Products: -
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?
furylacryloyl-Phe-Val + H2O
furylacryloyl-Phe + Val
-
Substrates: -
Products: -
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?
FVNQHLCGSHLV + H2O
FVNQHLCGSH + L-Leu-L-Val + L-Val
-
Substrates: -
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FVNQHLCGSHLVEAL + H2O
FVNQHLCGSHLVE + L-Ala-L-Leu + L-Leu
-
Substrates: -
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Glu-Asp-Glu-Phe-Phe-Leu-Ala + H2O
Glu-Asp-Glu-Phe-Phe-Leu + Ala
Substrates: -
Products: -
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?
Gly-L-Tyr + H2O
Gly + L-Tyr
Substrates: 1.6% hydrolysis
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isoaspartyl peptides + H2O
isoaspartyl dipeptides
-
Substrates: -
Products: -
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L-Ala-Gly-Gly + H2O
L-Ala-Gly + Gly
Substrates: 1.0% hydrolysis
Products: -
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L-Leu-L-Leu + H2O
L-Leu + L-Leu
Substrates: 57% hydrolysis
Products: -
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?
L-Lys-L-Tyr-L-Lys + H2O
L-Lys-L-Tyr + L-Lys
Substrates: 53% hydrolysis
Products: -
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?
L-Phe-L-Ala + H2O
L-Phe + L-Ala
Substrates: 16% hydrolysis
Products: -
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?
L-Thr-L-Val-L-Leu + H2O
L-Thr-L-Val + L-Leu
Substrates: 100% hydrolysis
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?
L-Val-L-Met + H2O
L-Val + L-Met
Substrates: 18% hydrolysis
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?
L-Val-L-Tyr + H2O
L-Val + L-Tyr
Substrates: 12% hydrolysis
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?
lysosomal neuraminidase-1 + H2O
?
Substrates: lysosomal neuraminidase-1 gains full catalytic activity in the lysosome through its binding to PPCA
Products: -
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?
N-((S)-5-amino-5-(carbamoyl)pentyl)-3-(aminooxymethyl)benzamide + H2O
?
Substrates: -
Products: -
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?
N-(2-furanacryloyl)-Phe-Phe + H2O
N-(2-furanacryloyl)-Phe + Phe
-
Substrates: -
Products: -
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?
N-acetyl-renin tetradecapeptide + H2O
?
-
Substrates: -
Products: -
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?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-Tyr + p-nitroaniline
-
Substrates: -
Products: -
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?
N-benzoyl-L-tyrosyl-4-nitroanilide + H2O
N-benzoyl-L-tyrosine + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
N-benzyloxycarbonyl-L-phenylalanyl-L-leucine+ H2O
N-benzyloxycarbonyl-L-phenylalanine + L-leucine
Substrates: -
Products: -
Products: -
?
N-carbobenzoxy-L-Phe-L-Ala + H2O
N-carbobenzoxy-L-Phe + L-Ala
-
Substrates: -
Products: -
Products: -
?
pancreatic carboxypeptidase A + H2O
hydrolyzed carboxypeptidase A + C-terminal amino acid
-
Substrates: -
Products: -
Products: -
?
pancreatic carboxypeptidase B + H2O
hydrolyzed pancreatic carboxypeptidase B + C-terminal amino acid
-
Substrates: -
Products: -
Products: -
?
poly-alpha-L-aspartic acid + H2O
?
-
Substrates: slowly
Products: -
Products: -
?
poly-alpha-L-glutamic acid + H2O
glutamic acid
-
Substrates: -
Products: -
Products: -
?
succinyl-L-Ile-L-Ile-L-Trp-7-amido-4-methylcoumarin + H2O
succinyl-L-Ile-L-Ile-L-Trp + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-enkephalin + H2O
?
Substrates: 89% hydrolysis
Products: -
Products: -
?
6-aminoquinoline-N-hydroxysuccimidyl carbamoyl-enkephalin + H2O
?
Substrates: 100% hydrolysis at pH 5.5
Products: -
Products: -
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitrolaniline
-
Substrates: -
Products: -
Products: -
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitrolaniline
-
Substrates: -
Products: -
Products: -
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
Substrates: -
Products: -
Products: -
?
benzoyl-Gly-beta-phenyllactate + H2O
?
-
Substrates: -
Products: -
Products: -
?
benzoyl-Gly-beta-phenyllactate + H2O
?
-
Substrates: poor substrate
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
-
Substrates: isoenzyme MpiCP-1
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
-
Substrates: 76% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
Substrates: isoenzyme MpiCP-1
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
Substrates: 119% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
Substrates: 150% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
Substrates: isoenzyme MpiCP-1
Products: -
Products: -
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
Substrates: 100% activity
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
Substrates: 17% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
Substrates: -
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
Substrates: poor substrate
Products: -
Products: -
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
Substrates: 21% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
-
Substrates: 59% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
-
Substrates: 309% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
Substrates: isoenzyme MpiCP-1
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
Substrates: 77% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
Substrates: 219% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
Substrates: 24% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: isoenzyme MpiCP-1
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: isoenzyme MpiCP-2
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: 21% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: 483% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
-
Substrates: 12% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
-
Substrates: 18% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
-
Substrates: 114% activity compared to benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
-
Substrates: preferred substrate for isoenzyme MpiCP-1
Products: -
Products: -
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
-
Substrates: preferred substrate for isoenzyme MpiCP-2
Products: -
Products: -
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
-
Substrates: 134% of the activity with benzyloxycarbonyl-Glu-Tyr
Products: -
Products: -
?
carboxypropionyl-Phe-4-nitroanilide + H2O
carboxypropionyl-Phe + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
carboxypropionyl-Phe-4-nitroanilide + H2O
carboxypropionyl-Phe + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
endothelin I + H2O
endothelin(1-20) + Trp
-
Substrates: containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
Products: -
Products: -
?
endothelin I + H2O
endothelin(1-20) + Trp
-
Substrates: containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
Products: -
Products: -
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
-
Substrates: -
Products: -
Products: -
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
-
Substrates: -
Products: -
Products: -
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-(3-[2-furyl]acryloyl)-L-Phe-L-Phe + H2O
N-(3-[2-furyl]acryloyl)-L-Phe + L-Phe
-
Substrates: -
Products: -
Products: -
?
N-(3-[2-furyl]acryloyl)-L-Phe-L-Phe + H2O
N-(3-[2-furyl]acryloyl)-L-Phe + L-Phe
Saccharomyces cerevisiae KPY382
-
Substrates: -
Products: -
Products: -
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
phytochelatin + H2O
phytochelatin 2 + ?
-
Substrates: -
Products: -
Products: -
?
phytochelatin + H2O
phytochelatin 2 + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: BRS1 may be involved in an early proteolytic step important for brassinosteroid perception
Products: -
Products: -
?
additional information
?
-
-
Substrates: splits off most readily aromatic and aliphatic amino acid residues at the carboxyl end
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic mechanism specificity overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: owing to its low specificity very suitable for sequence analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycine is split off very slowly
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of benzyloxycarbonyl-Gly-Pro
Products: -
Products: -
?
additional information
?
-
-
Substrates: neutral, basic and acid amino acids including proline are all hydrolyzed to approximately the same extent
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic mechanism specificity overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not cleave the MBPMu4 peptide VVHPFPPIVTPPPP
Products: -
Products: -
?
additional information
?
-
-
Substrates: cis regulation of serine carboxypeptidase I
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: Scpep1 has carboxypeptidase activity against endothelin ET-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: overview: synthetic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: no effect on the activity of malate dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity towards substrates with basic P1 amino acid residues is drastically increased by mutational replacement of Leu178
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural requirements for nucleophilic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the mechanism involves a charge-relay system in the hydrolysis of peptide and ester substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: inactivation of phosphoribosyltransferase
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic mechanism specificity overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrates overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: mechanism of carboxypeptidase-Y-catalyzed peptide semisynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: studies on hydrolytic properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of poly-L-lysine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of poly-L-proline
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the C-terminal processing of peptides and proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the degradation of biologically active peptide amides
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: CPD-Y can be used to specifically modify the C-terminus of peptides and proteins, for example biotinylation of antibodies at their C-termini
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not hydrolyze L-Ala-L-Leu, L-Val-L-Pro, L-Asp-L-Asp, and L-Arg-Gly-L-Asp
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme is not degrading D-amino acid-containing peptides, e.g. AQC-L-Tyr-D-Ala-Gly-L-Phe-D-Leu
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity towards benzyloxycarbonyl-Gly-Pro, benzoyl-Gly-Lys, and benzyloxycarbonyl-Pro-Pro
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic mechanism specificity overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: BRS1 may be involved in an early proteolytic step important for brassinosteroid perception
Products: -
Products: -
?
additional information
?
-
-
Substrates: cis regulation of serine carboxypeptidase I
Products: -
Products: -
?
additional information
?
-
-
Substrates: Scpep1 has carboxypeptidase activity against endothelin ET-1
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the C-terminal processing of peptides and proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the degradation of biologically active peptide amides
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CuCl
CuCl2
FeCl2
FeCl3
additional information
additional information
-
the enzyme does not require metals for activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
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
-
-
benzyloxycarbonyl-L-phenylalanyl chloromethane
-
diisopropylphosphorofluoridate-inactivated enzyme does not react with the inhibitor
carboxypeptidase Y inhibitor from baker's yeast
-
MW 23400-24000, purification, chemical and physical properties
-
D-Amino acids
-
less inhibitory than the L-enantiomers, non-competitive or mixed-type
E-64
-
1 mM, 10% inhibition, isoenzyme MpiCP-2; 1 mM, 22% inhibition, isoenzyme MpiCP-1
leupeptin
-
1 mM, 24% inhibition, isoenzyme MpiCP-1; 1 mM, 60% inhibition, isoenzyme MpiCP-2
N-(N-[1-trans-3-carboxyoxiran-2-carbonyl]-L-leucyl)-agmatine
-
93% residual activity at 1 mM
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
phosphoramidon
-
1 mM, 17% inhibition, isoenzyme MpiCP-1; 1 mM, 41% inhibition, isoenzyme MpiCP-2
Tfs1p
-
NatB-dependent acetylation is essential for the inhibitory activity on carboxypeptidase Y
-
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
diisopropyl fluorophosphate
-
benzyloxycarbonyl-L-phenylalanyl chloromethane-inhibited enzyme does not react with the inhibitor
diisopropylfluorophosphate
-
1 mM, 39% inhibition, isoenzyme MpiCP-1; 1 mM, 67% inhibition, isoenzyme MpiCP-2
diisopropylfluorophosphate
-
complete inhibition at 5 mM, at 30°C and pH 3.1
ebelactone B
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
Nalpha-tosyl-L-Lys-chloromethyl ketone
-
1 mM, 13% inhibition, isoenzyme MpiCP-2
Nalpha-tosyl-L-Phe-chloromethyl ketone
-
1 mM, 12% inhibition, isoenzyme MpiCP-2
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: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
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
pepstatin A
-
1 mM, 11% inhibition, isoenzyme MpiCP-2; 1 mM, 19% inhibition, isoenzyme MpiCP-1
Phenylmethylsulfonylfluoride
-
1 mM, 61% inhibition, isoenzyme MpiCP-1; 1 mM, complete inhibition, isoenzyme MpiCP-2
piperastatin A
-
1 mM, 17% inhibition, isoenzyme MpiCP-2; 1 mM, 87% inhibition, isoenzyme MpiCP-1
piperastatin A
-
IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 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
-
CathA inhibitor affects spermatophore wall digestion
-
additional information
-
not inhibited by trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Phenyl-1-propanol
-
inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe
CH3-CH2-CH2-CH2-Hg
-
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
CH3-CH2-CH2-Hg
-
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
Kar2p, Pdi1p, Ero1p
-
co-expression of Kar2p, Pdi1p and Ero1p give a synergistic effect on CPY expression, of which activity is 1.7times higher than that of the control strain
-
Karp2
-
a single co-expression of Kar2p leads to a 28% enhancement in extracellular CPY activity, relative to the control strain
-
proteinase A
-
active proteinase A is essential to the activity of carboxypeptidase Y
-
proteinase K
-
converts the proenzyme to the mature, active enzyme
-
additional information
-
FUSCA, a B3 domain transcription factor that lacks the N-terminal activation and B1 domain 3 activates the phaseolin promoter in the presence of abscisic acid
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.363
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine
-
-
0.61
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
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
1.1
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25°C, wild-type enzyme anf mutant enzyme C341V
additional information
additional information
-
kinetic characterization of peptide semisynthesis
-
additional information
additional information
-
overview: synthetic substrates
-
additional information
additional information
-
influence of mercurials
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
237
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine
-
-
1777
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
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
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
acetyl-D-Phe ethyl ester
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
1.7
benzyloxycarbonyl-D-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
0.3
benzyloxycarbonyl-D-Phe-D-Leu
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00538
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
0.000005
(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
0.00002 - 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
0.029 - 0.089
poststatin
Saccharomyces cerevisiae
-
IC50 at pH 5.6:0.089 mM, IC50 at pH 6.5: 0.029 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzymatic activity is significantly higher in the mating period of Eriocheir sinensis parallel to the latest developmental stage of the gland
additional information
enzymatic activity increases with maturation of cathepsin A to the 51.1 kDa form
additional information
-
enzymatic activity increases with maturation of cathepsin A to the 51.1 kDa form
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6 - 7
-
hydrolysis of peptides containing only neutral amino acids, e.g. benzyloxycarbonyl-Phe-Pro, benzyloxycarbonyl-Gly-Phe, benzyloxycarbonyl-Phe-Leu, benzoyl-Gly-Phe, acetyl-Phe-Leu
5.5
-
peptides containing an acidic amino acid, e.g. benzyloxycarbonyl-Phe-Glu, and benzyloxycarbonyl-Glu-Phe
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
-
pH 4.5: about 70% of activity maximum, pH 6: about 55% of activity maximum
5 - 6
-
pH 5.0: about 40% of maximal activity, pH 6.0: about 40% of maximal activity, hydrolysis of furyacryloyl-Phe-Ala
5 - 7
-
pH 5.0: about 45% of maximal activity, pH 7.0: about 50% of maximal activity, hydrolysis of hippuryl-L-beta-phenyllactate
5 - 9
-
pH 5.0: about 45% of maximal activity, pH 9.0: about 75% of maximal activity, hydrolysis of acetyl-Phe ethyl ester
5.5 - 8
-
pH 5.5: about 50% of maximal activity, pH 8.0: about 35% of maximal activity, hydrolysis of benzoyl-Tyr-4-nitroanilide
5.5 - 8.5
-
pH 5.5: about 50% of maximal activity, pH 8.0: about 60% of maximal activity, hydrolysis of benzyloxycarbonyl-Phe-NH2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30°C: about 45% of maximal activity, 55°C: 75% of maximal activity, hydrolysis of furyacryloyl-Phe-Ala
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
647191, 647192, 647206, 647218, 647223, 647224, 647225, 647226, 647227, 647228, 647229, 647230, 663479, 665058, 665316, 665563
-
-
brenda
-
677412, 677521, 677947, 678037, 678817, 679755, 679852, 679926, 680178, 680774, 681641, 681642, 681922, 681941, 681977, 682540, 682934, 683009
-
-
brenda
baker's yeast
30703, 647189, 647195, 647201, 647202, 647207, 647208, 647209, 647210, 647212, 647213, 647215, 647216, 647217, 647221, 647222
-
-
brenda
carboxypeptidase Y
-
-
brenda
small differences in amino acid composition and enzymatic properties between the enzyme from Danish yeast and the corresponding enzyme from Fleischmann yeast suggest the existence of more than 1 form of this enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SmSCP-1 is nearly 2fold in female fat body compared to male fat body
brenda
from a galactosialidosis patient transformed with simian virus-40-adenovirus recombinant
brenda
a cDNA of bone marrow-derived monocyte/macrophage osteoclast progenitors is used
brenda
-
highly expressed in spleen, followed by brain, intestine, and stomach
brenda
additional information
-
highly expressed in spleen, followed by brain, intestine, and stomach
brenda
-
from Peptech, Hilleroed, Denmark
brenda
-
highly expressed in spleen, followed by brain, intestine, and stomach
brenda
-
highly expressed in spleen, followed by brain, intestine, and stomach
brenda
additional information
ubiquitously expressed in all examined healthy tissues, high expression levels in head kidney and intestine, lowest expression level in blood
brenda
additional information
-
ubiquitously expressed in all examined healthy tissues, high expression levels in head kidney and intestine, lowest expression level in blood
brenda
additional information
-
SmSCP-1 is upregulated nearly four-fold in the female midges compared to males. SmSCP-1 mRNA is not detected in the midgut
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
small amount also present in cytosolic fraction of transfected HEK-293 cells
brenda
-
recombinant enzyme expressed in Escherichia coli
brenda
membrane bound compartments between nucleus and kinetoplast
-
brenda
-
membrane bound compartments between nucleus and kinetoplast
-
-
brenda
-
the enzyme is synthesized on ribosomes and sorted into vacuoles. The vacuolar localization signal Gln24-Arg-Pro-Leu27 is loacetd near the NH2-terminus of the propeptide
brenda
-
the localization determinant resides in the propeptide of the enzyme
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
mice with a double CathA/Scpep1 deficiency (DD mice) demonstrate hypertension, increased ET-1-induced vasoconstriction and prolonged half-life of circulating ET-1 as compared to both wild-type animals and those with single CathA or Scpep1 deficiencies
malfunction
-
cells deficient in both enzymes Prc1 and Ybr139w have defects in autophagy-dependent protein synthesis, vacuolar zymogen activation, and autophagic body breakdown. Deletion of PRC1 or both PRC1 and YBR139W almost completely abolishes carboxypeptidase Y activity, whereas deletion of YBR139W alone has little to no effect
malfunction
Saccharomyces cerevisiae KPY382
-
cells deficient in both enzymes Prc1 and Ybr139w have defects in autophagy-dependent protein synthesis, vacuolar zymogen activation, and autophagic body breakdown. Deletion of PRC1 or both PRC1 and YBR139W almost completely abolishes carboxypeptidase Y activity, whereas deletion of YBR139W alone has little to no effect
-
physiological function
-
Btn1p is required for vacuole protein sorting of Cpy1p
physiological function
-
cathepsin A is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human antigen-presenting cells
physiological function
Scpep1-deficient mice are viable and fertile, and do not exhibit either lysosomal storage or reduced lysosomal serine carboxypeptidase activity
physiological function
-
Scpep1 and CathA together participate in the control of endothelin ET-1 regulation of vascular tone and hemodynamics
physiological function
-
cathepsin A (cathA) is involved in spermatophore wall rupture
physiological function
CtsA has potentially important roles in innate immune responses of turbot. Recombinant CTSA binds lipopolysaccharide with high affinity, and lipoteichoic acid and peptidoglycan with relatively low affinity
physiological function
-
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
physiological function
mouse model of cardiomyocyte-specific human CTSA overexpression. CTSA strongly impairs the balance of the proteolytic system by upregulating proteases such as cathepsin B, cathepsin D, and cathepsin Z while downregulating numerous protease inhibitors. Cardiomyocyte-specific human CTSA overexpression strongly reduces the levels of numerous antioxidative stress proteins, i.e., peroxiredoxins and protein deglycase DJ-1. In vitro, using cultured rat cardiomyocytes, ectopic overexpression of CTSA results in accumulation of reactive oxygen species
physiological function
-
the enzymes Ybr139w and Prc1 have important roles in proteolytic processing in the vacuole and the terminal steps of autophagy
physiological function
Saccharomyces cerevisiae KPY382
-
the enzymes Ybr139w and Prc1 have important roles in proteolytic processing in the vacuole and the terminal steps of autophagy
-
Show AA Sequence and Transmembrane Helices (577 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
41100 - 54700
-
SDS-PAGE, the number of subunits among phaseolins varies from 2 to 6 with a specific molecular weight for each subunit ranging from 54700 to 41100 Da depending on the cultivar investigated
50000
51100
MALDI-TOF, mature protein. Enzymatic activity increases with maturation of Cathepsin A to the 51.1 kDa form
61000
67000
additional information
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
additional information
consisting of a 35 kDa N-terminal fragment and a 18 kDa C-terminal fragment, the two-chain form of Scpep1 does not form disulfide bridges
additional information
-
consisting of a 35 kDa N-terminal fragment and a 18 kDa C-terminal fragment, the two-chain form of Scpep1 does not form disulfide bridges
additional information
-
SDS-PAGE, the number of subunits among phaseolins varies from 2 to 6 with a specific molecular weight for each subunit ranging from 54700 to 41100 Da depending on the cultivar investigated
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
-
fusion with the N-terminal half of the Zea mays prolamin gamma-zein forms endoplasmic reticulum-located protein bodies
glycoprotein
-
the carbohydrate moiety has a slightly protective role in heat-induced unfolding and highly protective role the enzyme against pressure induced denaturation
glycoprotein
-
the enzyme is synthesized as a prepro-form that travels through the endoplasmic reticulum and Golgi to its final destination in vacuoles. Various post-translational events have been identified, e.g. carbohydrate modification and cleavage of the presegments. Core glycosylation occurs to a 67000 Da form called p1-CPY. Oligosaccharide modification is completed to give p2-CPY, 69000 Da, in which 2 N-acetyl-glucosamines and 8-14 mannoses, including a 1 mannosyl-phosphate group are attached
glycoprotein
-
25.3% carbohydrate, mannose 83.3% by weight, glucosamine 10.3%, with traces of galactose and galactosamine
glycoprotein
-
16 residues of glucosamine and about 15% hexose
glycoprotein
-
structural integrity and functional activity is influenced by its associated carbohydrate component
glycoprotein
-
the native enzyme is a glycoprotein whereas the recombinant enzyme produced from Escherichia coli is not glycosylated. The glycosylation does not greatly affect the enzymatic activity. Glycosylation is required for efficient intracellular transport of the enzyme but not for vacuolar sorting, in vivo stability or activity
glycoprotein
-
CPY shows microheterogeneity in N-glycans such as Man11-15GlcNAc2 at Asn13, Man8-12GlcNAc2 at Asn87, Man9-14GlcNAc2 at Asn168 and phosphorylated Man12-17GlcNAc2 as well as Man11-16GlcNAc2 at Asn368. In vacuoles the steady release of mannose/phosphomannose residues from glycans may occur initially at Asn13 or Asn168 followed by at Asn368
glycoprotein
-
enzyme Prc1 is N-glycosylated at Asn124, Asn198, Asn279, and Asn479. Enzyme Ybr139w is N-glycosylated at Asn163 and Asn242.
glycoprotein
Saccharomyces cerevisiae KPY382
-
enzyme Prc1 is N-glycosylated at Asn124, Asn198, Asn279, and Asn479. Enzyme Ybr139w is N-glycosylated at Asn163 and Asn242.
-
proteolytic modification
the activation of precursor cathepsin A is achieved by proteolytic removal of a larger 3.3-kDa peptide that includes the blocking peptide, bypassing the requirement for conformational changes
proteolytic modification
-
the gene for carboxypeptidase Y, PRC1, encodes an inactive pre-pro-enzyme with a 20 residue signal peptide, a 91 residue propeptide and a 421 residue mature region. When the newly synthesized carboxypeptidase Y is translocated to the endoplasmic reticulum membrane, the signal peptide is removed by a signal peptidase. In the lumen of the endoplasmic reticulum, the processed protein undergoes folding. Maturation proceeds in the vacuoles where the pro segment of pro-CPY is cleaved by several vacuolar hydrolases, including proteinase A and proteinase B and aminopeptidase. Proteinase A is considered to be the first step in the activation cascade of proCPY in which the protein is cleaved leaving the C-terminal 35 amino acid residue portion of the pro-segment attached to the mature CPY. Subsequently proteinase B is involved in further processing to leave 5 residues attached to the mature CPY. The reamaining 5 residues are finally removed by aminopeptidase
proteolytic modification
-
structural integrity and functional activity is influenced by its associated carbohydrate component
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mature cathepsin A is determined to 2.8 A resolution
crystal structures show that the structure of mature Cathepsin A is identical to the structure of the precursor and that activation depends solely on the removal/disorder transition of the activation domain. The active catalytic domain is held together by a strategically located disulfide bridge, linking the loose ends that are formed after removal/disorder transition of the activation domain
sitting drop vapour diffusion method with 0.2 M potassium thiocyanate and 20% PEG 3350
-
carboxypeptidase Y inhibitor IC complexed with carboxypeptidase Y, hanging-drop vapour-diffusion method
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hanging-drop vapor diffusion method, crystal strcuture of the carboxypeptidase Y inhibitor Ic in complex with carboxypeptidase Y at 2.7 A resolution
significance of Thr60 and Met398 in hydrolysis and aminolysis reactions
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
C262A
the mutant shows 8.5% and 1.8% activity with N-benzyloxycarbonyl-L-phenylalanyl-L-leucine and N-benzoyl-L-tyrosyl-4-nitroanilide, respectively, compared to the wild type enzyme
C268A
the mutant shows 16% and 1.9% activity with N-benzyloxycarbonyl-L-phenylalanyl-L-leucine and N-benzoyl-L-tyrosyl-4-nitroanilide, respectively, compared to the wild type enzyme
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
D415A
-
the mutation drastically reduces the activity of Ybr139w compared to the wild type enzyme
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
H474A
-
the mutation drastically reduces the activity of Ybr139w compared to the wild type enzyme
H508A
-
the mutation drastically reduces the activity of Prc1 compared to the wild type enzyme
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/L272A
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
L272D
L272E
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
L272Q
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
L272R/M398F
L272R/T60F
N87I
-
mutant enzyme with reduced transport rate and reduced enzymatic activity, 30%
S219A
-
the mutation drastically reduces the activity of Ybr139w compared to the wild type enzyme
S257A
-
the mutation drastically reduces the activity of Prc1 compared to the wild type enzyme
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
S297D
S297E
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
S297Q
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
T60F/L267D/L272A
D415A
Saccharomyces cerevisiae KPY382
-
the mutation drastically reduces the activity of Ybr139w compared to the wild type enzyme
-
H474A
Saccharomyces cerevisiae KPY382
-
the mutation drastically reduces the activity of Ybr139w compared to the wild type enzyme
-
H508A
Saccharomyces cerevisiae KPY382
-
the mutation drastically reduces the activity of Prc1 compared to the wild type enzyme
-
S219A
Saccharomyces cerevisiae KPY382
-
the mutation drastically reduces the activity of Ybr139w compared to the wild type enzyme
-
S257A
Saccharomyces cerevisiae KPY382
-
the mutation drastically reduces the activity of Prc1 compared to the wild type enzyme
-
nutrition
-
the enzyme can be used to eliminate the bitterness of bitter peptides
additional information
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
the gene vps4 null mutant missorts the vacuolar enzyme carboxypeptidase Y
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
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 6
-
at pH 3.1, its relative activity is maintained (70%), the enzyme remains stable in the pH range of 2-6 at 30°C for 30 min
2 - 8
4 - 6
7
-
at temperatures above 25°C the enzyme is most stable at pH 7.0
additional information
-
rapid and irreversible inactivation at low pH
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 50
-
the enzyme activity remained intact at temperatures below 45°C, but declined rapidly at temperatures exceeding 50°C
50
55
60
additional information
-
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5°C, it undergoes an irreversible inactivation in which nearly 50% of the alpha-helical structure is lost as judged by circular dichroism spectral analysis. When the applied pressure is limited to below 200 mPa, the cold inactivation process appears to be reversible. In the presence of reducing agent, this reversible phenomenon, observed at below 200 mPa, diminishes to give an inactive enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pressure-induced denaturation is a process involving at least three transitions. Low pressure, below 150 mPa, induces slight conformational changes characterized by a slight decrease in the center of the spectral mass of intrinsic fluorescence, whereas no changes in 8-anilino-1-naphthalene sulfonic acid binding fluorescence are observed and 80% of the catalytic activity remains. Higher pressure, 150-500 mPa, induce further conformatiinal changes, characterized by a large decrease in the center of the spectral mass of intrinsic fluorescence, a large increase in the 8-anilino-1-naphthalene sulfonic acid binding fluorescence and the loss of all catalytic activity. A further increase in pressure, above 550 mPa induces transition from this first molten globule-like state to a second malten globule-like state. A similar three-transition process is found for unglycosylated carboxypeptidase Y, but the first two transitions clearly occur at lower pressures than those for glycosylated carboxypeptidase Y
-
the carboxypeptidase Y is composed of two structural domains which unfold independently, procarboxypeptidase Y behaves as a single domain, thus ensuring cooperative unfolding. The carbohydrate moiety has a slightly protective role in heat-induced unfolding and highly protective role in pressure-induced unfolding
-
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5°C, it undergoes an irreversible inactivation in which nearly 50% of the alpha-helical structure is lost as judged by circular dichroism spectral analysis. When the applied pressure is limited to below 200 mPa, the cold inactivation process appears to be reversible. In the presence of reducing agent, this reversible phenomenon, observed at below 200 mPa, diminishes to give an inactive enzyme
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Toyopearl butyl-650M column chromatography
Butyl-Toyopearl 650C column chromatography and DEAE Sephadex A-50 gel filtration
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development of a novel method that can produce active yeast enzyme from inactive inclusion bodies expressed in escherichia coli
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Mono S cation exchange column chromatography and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. The native enzyme is a glycoprotein whereas the recombinant enzyme produced from Escherichia coli is not glycosylated
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
After Aeromonas hydrophila infection, CtsA is significantly upregulated in lung, heart, muscle, and kidney and is downregulated in liver, spleen, and intestine, and exhibits no significant changes in stomach and skin
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
efficient folding of carboxypeptidase Y is dependent on the presence of the proregion. Thus denatured pro-carboxypeptidase Y, in contrast to the mature enzyme, refolds efficiently in vitro in low ionic strength buffers. Under these conditions denatured mature carboxypeptidase Y forms an inactive, soluble folding intermediate
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the denatured His-tagged carboxypeptidase propeptide is refolded by dilution 1:60 into the renaturation buffer, 50 mM Tris-HCl containing 0.5 M NaCl and 3 mM EDTA, pH 8.0. The denatured carboxypeptidase is refolded by dilution 1:60 into the reanturation buffer containing containing His-tagged carboxypeptidase propeptide at various concentrations. Increasing the molar ratio of His-tagged carboxypeptidase propeptide to carboxypeptidase results in an increase in the carboxypeptidase refolding yield, indicating that the His-tagged carboxypeptidase propeptide plays a chaperone-like role in in vitro folding of the carboxypeptidase. When refolding is carried out in the presence of 10 molar equivalent His-tagged carboxypeptidase propeptide the specific activity, N-(2-furanacryloyl)-Phe-Phe hydrolysis activity per mg of protein, is 63% of that of the native enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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application of CPY as sensing element in a biosensor for the direct detection of ochratoxin A and comparison with thermolysin. Thermolysin and CPY both exhibit an optimal activity under the conditions 35 min cross-linking time, working pH of 7 and temperature of 25°C and exhibit comparable analytical performances in the biosensor. Ochratoxin A concentrations can be determined without pretreatment of the sample and no matrix effect is observed
molecular biology
a method is described exploiting the possibility to attach different reactive handles to their C-termini using a reaction catalyzed by CPY. It is possible to attach pairs of reaction handles which can react with each other to each of the peptides to be coupled. In a second step, the two modified peptides can be linked together by a chemical reaction, such as an oxime-forming reaction or a copper(I) catalyzed (2+3)-cycloaddition reaction of an azide with an alkyne
nutrition
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MpiCP-1 suppresses and reverses the development of the bitterness taste that results from the pepsin hydrolysis of soybean protein by releasing mainly hydrophobic amino acids from the C-termini of the bitter components
synthesis
synthesis of CPY in Pichia pastoris as procarboxypeptidase Y with a yield of about 605 mg/l in shake-flasks after 168 h induction with 1 % (v/v) methanol. This precursor is cleaved by endogenous proteinases of Pichia pastoris and released into the fermentation broth as active carboxypeptidase Y within 2 weeks at 10°C. The recombinant enzyme is optimally active at 30°C and pH 6.0, with an optimal activity of about 305 U/mg
EXTERNAL LINKS (specific for EC-Number 3.4.16.5)
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Release 2026.1 (March 2026)
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