Information on EC 3.4.16.5 - carboxypeptidase C

New: Word Map on EC 3.4.16.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.16.5
-
RECOMMENDED NAME
GeneOntology No.
carboxypeptidase C
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of a C-terminal amino acid with broad specificity
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
hydrolysis of peptide bond
Q6Y3Z8
carboxyterminal bond
hydrolysis of peptide bond
Trypanosoma cruzi Y
-
carboxyterminal bond
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.4.16.1
-
formerly
A-type metallocarboxypeptidase
-
-
acidic serine carboxypeptidase
-
-
carboxypeptidase a
-
-
carboxypeptidase a
Phaffia rhodozyma CBS 5905
-
-
-
carboxypeptidase A4
-
-
carboxypeptidase C
-
-
carboxypeptidase C
-
-
-
Carboxypeptidase II
-
-
carboxypeptidase Y
-
-
-
-
carboxypeptidase Y
-
-
carboxypeptidase Y
-
-
carboxypeptidase Y
-
-
carboxypeptidase Y
Saccharomyces cerevisiae BJ2168, Saccharomyces cerevisiae BY4741, Saccharomyces cerevisiae EOS1
-
-
-
carboxypeptidase Y
-
-
carboxypeptidase YSCY
-
-
-
-
carboxypeptidase-Y
-
-
CathA
-
-
cathepsin A
-
-
-
-
CP-MI
-
-
-
-
CP-MIII
-
-
-
-
CP-WIII
-
-
-
-
CPA4
-
-
CPY
-
-
-
-
CPY
Saccharomyces cerevisiae BJ2168, Saccharomyces cerevisiae BY4741
-
-
-
deamidase
-
-
-
-
EC 3.4.12.1
-
-
formerly
-
hCath A
-
-
lysosomal carboxypeptidase A
-
-
-
-
lysosomal carboxypeptidase A
-
-
lysosomal protective protein
-
-
-
-
lysosomal protective protein
-
-
MpiCP-2
-
-
Phaseolin
-
-
-
-
PpcA
-
-
PpcA
-
-
PpcA
P16675
-
protective protein cathepsin A
-
-
protective protein/cathepsin A
-
-
protective protein/cathepsin A
P16675
-
retinoid-inducible serine carboxypeptidase
-
-
Scpep1
Q920A5
formerly retinoid-inducible serine carboxypeptidase
Ser carboxypeptidase
-
-
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 carboxpeptidase
Q6Y3Z8
-
serine carboxpeptidase
Trypanosoma cruzi Y
Q6Y3Z8
-
-
serine carboxypeptidase
-
-
serine carboxypeptidase
-
-
-
serine carboxypeptidase 1
Q920A5
-
serine carboxypeptidase I
-
-
-
-
serine carboxypeptidase I
-
-
serine carboxypeptidase Scpep1
-
-
TcCBP
Q6Y3Z8
-
TcCBP
Trypanosoma cruzi Y
Q6Y3Z8
-
-
MO54
-
-
-
-
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
CAS REGISTRY NUMBER
COMMENTARY
9046-67-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aspergillus niger CDP-AI
CDP-AI
-
-
Manually annotated by BRENDA team
Citrus sp.
; orange
-
-
Manually annotated by BRENDA team
isoenzyme MpiCP-1; isoenzyme MpiCP-2
-
-
Manually annotated by BRENDA team
IFO 4478
-
-
Manually annotated by BRENDA team
cultivars Malviya-36 and Pant-12
-
-
Manually annotated by BRENDA team
strain CBS 5905
-
-
Manually annotated by BRENDA team
Phaffia rhodozyma CBS 5905
strain CBS 5905
-
-
Manually annotated by BRENDA team
baker's yeast; baker's yeast (inactive form)
-
-
Manually annotated by BRENDA team
baker's yeast; 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
-
-
Manually annotated by BRENDA team
strain BJ2168
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae BJ2168
strain BJ2168
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae EOS1
strain EOS1
-
-
Manually annotated by BRENDA team
CDP-MIII and CDP-MI
-
-
Manually annotated by BRENDA team
strain Y
SwissProt
Manually annotated by BRENDA team
Trypanosoma cruzi Y
strain Y
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Q920A5
Scpep1-deficient mice are viable and fertile, and do not exhibit either lysosomal storage or reduced lysosomal serine carboxypeptidase activity
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu-Arg + H2O
5-dimethylaminonaphthalene-1-sulfonyl-Phe-Leu + Arg
show the reaction diagram
-
-
-
?
9-(R)-4'-(R)-[[[(S)-1-[(ethoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-2'-fluoro-1'-furanyladenine + H2O
?
show the reaction diagram
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu + Ala
show the reaction diagram
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu + Ala
show the reaction diagram
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu + Ala
show the reaction diagram
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu + Ala
show the reaction diagram
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu + Ala
show the reaction diagram
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu + Ala
show the reaction diagram
-
-
-
-
?
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Phe ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Phe-Leu + H2O
acetyl-Phe + Leu
show the reaction diagram
-
-
-
-
?
acetyl-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
Acetyl-Tyr ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Tyr-ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
adrenocorticotropic hormone fragment 7-38 + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Ala benzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Ala-OGly + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Ala-OMe + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitrolaniline
show the reaction diagram
Phaseolus vulgaris, Citrus sp.
-
-
-
-
?
benzoyl-Gly benzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
show the reaction diagram
-
isoenzyme MpiCP-2
-
-
?
benzoyl-Gly-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
-
-
benzoyl-Gly-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-beta-phenyllactate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
show the reaction diagram
-
isoenzyme MpiCP-2
-
-
?
benzoyl-Gly-OEt + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-OGly + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-OMe + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-OPhe + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Phe + H2O
benzoyl-Gly + Phe
show the reaction diagram
-
-
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzoyl-L-tyrosine-p-nitroanilide + H2O
benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
benzoyl-Phe-Gly + H2O
benzoyl-Phe + Gly
show the reaction diagram
-
-
-
-
?
benzoyl-Phe-OGly + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Phe-OMe + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala + H2O
benzyloxycarbonyl-Ala + Ala
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
show the reaction diagram
-
76% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Ala-Glu + H2O
benzyloxycarbonyl-Ala + Glu
show the reaction diagram
-
isoenzyme MpiCP-1, isoenzyme MpiCP-2
-
-
?
Benzyloxycarbonyl-Ala-Leu + H2O
Benzyloxycarbonyl-Ala + Leu
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg-Pro + H2O
benzyloxycarbonyl-Arg + Pro
show the reaction diagram
Citrus sp.
-
-
-
-
?
benzyloxycarbonyl-Glu-Leu + H2O
benzyloxycarbonyl-Glu + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
119% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
isoenzyme MpiCP-1
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
show the reaction diagram
-
150% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
show the reaction diagram
-
100% activity
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
show the reaction diagram
-
isoenzyme MpiCP-1, isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Gly-Arg + H2O
benzyloxycarbonyl-Gly + Arg
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Glu + H2O
benzyloxycarbonyl-Gly + Glu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
benzyloxycarbonyl-Gly-Gly + Phe
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
show the reaction diagram
-
17% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Gly-Met + H2O
benzyloxycarbonyl-Gly + Met
show the reaction diagram
-
19% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
show the reaction diagram
-
poor substrate
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
show the reaction diagram
-
21% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Gly-Pro + H2O
benzyloxycarbonyl-Gly + Pro
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
show the reaction diagram
-
59% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro-Leu + Gly
show the reaction diagram
-
309% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
benzyloxycarbonyl-Gly-Pro-Leu-Gly + Pro
show the reaction diagram
-
3% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Gly-Val + H2O
Benzyloxycarbonyl-Gly + Val
show the reaction diagram
-
24% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-His-Leu + H2O
benzyloxycarbonyl-His + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-His-Phe + H2O
benzyloxycarbonyl-His + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-His-Tyr + H2O
benzyloxycarbonyl-His + Tyr
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ile-Leu + H2O
benzyloxycarbonyl-Ile + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Leu + H2O
benzyloxycarbonyl-L-Phe + L-Leu
show the reaction diagram
P10619
-
-
-
?
benzyloxycarbonyl-Leu-Leu + H2O
benzyloxycarbonyl-Leu + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
show the reaction diagram
Citrus sp.
-
-
-
-
?
benzyloxycarbonyl-Nle-Leu + H2O
benzyloxycarbonyl-Nle + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
show the reaction diagram
-
77% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
show the reaction diagram
-
isoenzyme MpiCP-1, isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
show the reaction diagram
-
219% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-beta-Ala + H2O
benzyloxycarbonyl-Phe + beta-Ala
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Glu + H2O
benzyloxycarbonyl-Phe + Glu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
show the reaction diagram
-
24% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
show the reaction diagram
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Phe-His + H2O
benzyloxycarbonyl-Phe + His
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
21% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
isoenzyme MpiCP-1, isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
483% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Phe + H2O
benzyloxycarbonyl-Phe + Phe
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
show the reaction diagram
-
12% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
show the reaction diagram
-
18% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
Benzyloxycarbonyl-Phe-Tyr + H2O
Benzyloxycarbonyl-Phe + Tyr
show the reaction diagram
-
114% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Tyr-Gly + H2O
benzyloxycarbonyl-Phe-Tyr + Gly
show the reaction diagram
-
172% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Phe-Tyr-Leu + H2O
benzyloxycarbonyl-Phe-Tyr + Leu
show the reaction diagram
-
120% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Pro-Leu + H2O
benzyloxycarbonyl-Pro + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Pro-Leu + Gly
show the reaction diagram
-
isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Ser-Leu + H2O
benzyloxycarbonyl-Ser + Leu
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
show the reaction diagram
-
134% of the activity with benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Tyr-Glu + H2O
benzyloxycarbonyl-Tyr + Glu
show the reaction diagram
-
preferred substrate for isoenzyme MpiCP-1, preferred substrate for isoenzyme MpiCP-2
-
-
?
benzyloxycarbonyl-Tyr-Gly + H2O
benzyloxycarbonyl-Tyr + Gly
show the reaction diagram
-
188% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Tyr-Phe + H2O
benzyloxycarbonyl-Tyr + Phe
show the reaction diagram
-
201% activity compared to benzyloxycarbonyl-Glu-Tyr
-
-
?
benzyloxycarbonyl-Val-Leu + H2O
benzyloxycarbonyl-Val + Leu
show the reaction diagram
-
-
-
-
?
bombesin + H2O
?
show the reaction diagram
-
-
-
-
?
carboxypropionyl-Phe-4-nitroanilide + H2O
carboxypropionyl-Phe + 4-nitroaniline
show the reaction diagram
Phaseolus vulgaris, Citrus sp.
-
-
-
-
?
corn gluten + H2O
?
show the reaction diagram
-
-
-
-
?
corticotropin-releasing factor fragment 6-33 + H2O
?
show the reaction diagram
-
-
-
-
?
cyclo-statherin Q-37 + H2O
?
show the reaction diagram
-
-
-
-
?
endothelin I + H2O
endothelin(1-20) + Trp
show the reaction diagram
-
containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
-
-
-
endothelin I + H2O
endothelin(1-20) + Trp
show the reaction diagram
-
containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
-
-
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Glu + H2O
furylacryloyl-Ala + Glu
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Leu + H2O
furylacryloyl-Ala + Leu
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
show the reaction diagram
-
-
-
-
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
show the reaction diagram
-
-
-
-
?
furylacryloyl-Arg-Leu + H2O
furylacryloyl-Arg + Leu
show the reaction diagram
-
preferred substrate
-
-
?
furylacryloyl-Lys-Ala + H2O
furylacryloyl-Lys + Ala
show the reaction diagram
-
-
-
-
?
furylacryloyl-Lys-Leu + H2O
furylacryloyl-Lys + leu
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
-
furylacryloyl-Phe ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Phe
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Leu + H2O
furylacryloyl-Phe + Leu
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-NHEt + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-OGly + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-OMe + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Phe + H2O
furylacryloyl-Phe + Phe
show the reaction diagram
-
-
-
-
?
furylacryloyl-Phe-Val + H2O
furylacryloyl-Phe + Val
show the reaction diagram
-
-
-
-
?
FVNQHLCGSHLV + H2O
FVNQHLCGSH + L-Leu-L-Val + L-Val
show the reaction diagram
-
-
-
-
?
FVNQHLCGSHLVEAL + H2O
FVNQHLCGSHLVE + L-Ala-L-Leu + L-Leu
show the reaction diagram
-
-
-
-
?
Glu-Asp-Glu-Phe-Phe-Leu-Ala + H2O
Glu-Asp-Glu-Phe-Phe-Leu + Ala
show the reaction diagram
-
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-beta-phenyl lactate + H2O
?
show the reaction diagram
-
-
-
-
?
isoaspartyl peptides + H2O
isoaspartyl dipeptides
show the reaction diagram
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
show the reaction diagram
Phaseolus vulgaris, Citrus sp.
-
-
-
-
?
N-((S)-5-amino-5-(carbamoyl)pentyl)-3-(aminooxymethyl)benzamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(2-furanacryloyl)-Phe-Phe + H2O
N-(2-furanacryloyl)-Phe + Phe
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenyl-azoformyl)-L-Phe-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-renin tetradecapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
show the reaction diagram
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ2168
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-Tyr + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-L-Phe-L-Ala + H2O
N-carbobenzoxy-L-Phe + L-Ala
show the reaction diagram
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha
show the reaction diagram
Phaffia rhodozyma, Phaffia rhodozyma CBS 5905
-
-
-
-
?
oxidized insulin B + H2O
?
show the reaction diagram
-
-
-
-
?
pancreatic carboxypeptidase A + H2O
hydrolyzed carboxypeptidase A + C-terminal amino acid
show the reaction diagram
-
-
-
?
pancreatic carboxypeptidase B + H2O
hydrolyzed pancreatic carboxypeptidase B + C-terminal amino acid
show the reaction diagram
-
-
-
?
pepsin-digested soy protein + H2O
?
show the reaction diagram
-
-
-
-
?
phytochelatin + H2O
phytochelatin 2 + ?
show the reaction diagram
-
-
-
-
?
poly-alpha-L-aspartic acid + H2O
?
show the reaction diagram
-
slowly
-
-
-
poly-alpha-L-glutamic acid + H2O
glutamic acid
show the reaction diagram
-
-
-
?
succinyl-L-Ile-L-Ile-L-Trp-7-amido-4-methylcoumarin + H2O
succinyl-L-Ile-L-Ile-L-Trp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Tamm-Horsfall glycoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
trypsin-digested casein + H2O
?
show the reaction diagram
-
-
-
-
?
lysosomal neuraminidase-1 + H2O
?
show the reaction diagram
-
lysosomal neuraminidase-1 gains full catalytic activity in the lysosome through its binding to PPCA
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
Citrus sp.
-
-
-
-
-
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
?
-
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
?
-
-
inactivation of phosphoribosyltransferase
-
-
-
additional information
?
-
-
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
?
-
-
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
?
-
Phaseolus vulgaris, 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
?
-
-
mechanism of carboxypeptidase-Y-catalyzed peptide semisynthesis
-
-
-
additional information
?
-
Citrus sp.
-
neutral, basic and acid amino acids including proline are all hydrolyzed to approximately the same extent
-
-
-
additional information
?
-
-
studies on hydrolytic properties
-
-
-
additional information
?
-
-
no hydrolysis of poly-L-lysine, 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
?
-
-
BRS1 may be involved in an early proteolytic step important for brassinosteroid perception
-
-
-
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, 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
?
-
-
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
?
-
-
does not cleave the MBPMu4 peptide VVHPFPPIVTPPPP
-
-
-
additional information
?
-
Q920A5
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
-
-
-
-
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
?
-
-
BRS1 may be involved in an early proteolytic step important for brassinosteroid perception
-
-
-
additional information
?
-
-
cis regulation of serine carboxypeptidase I
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
As3+
-
marked increase of activity at 0.05 mM
CaCl2
-
1 mM, 18% inhibition, isoenzyme MpiCP-1
Cd2+
-
stimulates activity
CdCl2
-
1 mM, 18% inhibition, isoenzyme MpiCP-2
CoCl2
-
1 mM, 23% inhibition, isoenzyme MpiCP-1
CuCl
-
1 mM, 33% inhibition, isoenzyme MpiCP-1; 1 mM, 84% inhibition, isoenzyme MpiCP-2
CuCl2
-
1 mM, 36% inhibition, isoenzyme MpiCP-1; 1 mM, 73% inhibition, isoenzyme MpiCP-2
FeCl2
-
1 mM, 35% inhibition, isoenzyme MpiCP-1; 1 mM, 73% inhibition, isoenzyme MpiCP-2
FeCl3
-
1 mM, 37% inhibition, isoenzyme MpiCP-1; 1 mM, 86% inhibition, isoenzyme MpiCP-2
HgCl2
-
1 mM, complete inhibition, isoenzyme MpiCP-2
NiCl2
-
1 mM, 12% inhibition, isoenzyme MpiCP-2
PbCl2
-
1 mM, 47% inhibition, isoenzyme MpiCP-2
SnCl2
-
1 mM, 47% inhibition, isoenzyme MpiCP-2
Zinc
Citrus sp.
-
possibly contains zinc in the active site, orange peel
ZnSO4
-
1 mM, 46% inhibition, isoenzyme MpiCP-2
MgCl2
-
1 mM, 15% inhibition, isoenzyme MpiCP-1
additional information
-
the enzyme does not require metals for activity
additional information
Citrus sp.
-
no activation by metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-1-chloro-4-phenyl-3-tosylamido-2-butanone
-
37% residual activity at 1 mM
1,10-phenanthroline
-
-
1,2-epoxy-3-(p-nitrophenoxy)propane
-
1 mM, 14% inhibition, isoenzyme MpiCP-2
2,2'-dipyridyl
-
1 mM, 21% inhibition, isoenzyme MpiCP-1; 1 mM, 22% inhibition, isoenzyme MpiCP-2
2-mercaptoethanol
-
1 mM, 10% inhibition
2-mercaptoethanol
-
1 mM, 13% inhibition, isoenzyme MpiCP-2
2-propanol
Citrus sp.
-
above 5%
3,4-Dichloroisocoumarin
-
effective inhibitor
3-Phenyl-1-propanol
-
inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe
4-Aminobenzylsuccinic acid
-
-
acetyl-D-Phe
-
-
acetyl-D-Phe ethyl ester
-
-
acetyl-D-Phe-ethyl ester
-
-
benzyloxycarbonyl-D-Phe
-
-
benzyloxycarbonyl-D-Phe-D-Leu
-
-
benzyloxycarbonyl-Gly-Leu-Phe-CH2Cl
-
-
Benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
irreversible inhibition of peptidase and esterase activity, inhibition is retarded by the competitive inhibitors benzyloxycarbonyl-D-phenylalanine-D-leucine and trans-cinnamate
Benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
-
Benzyloxycarbonyl-L-phenylalanyl chloromethane
-
diisopropylphosphorofluoridate-inactivated enzyme does not react with the inhibitor
Benzyloxycarbonyl-Phe
-
-
beta-phenyl-L-lactate
-
-
Beta-phenylpropionate
-
-
CaCl2
-
1 mM, 16% inhibition
CaCl2
-
73% residual activity at 10 mM
carboxypeptidase inhibitor IC
-
-
-
carboxypeptidase Y inhibitor from baker's yeast
-
MW 23400-24000, purification, chemical and physical properties
-
carboxypeptidase Y inhibitor IC
-
-
-
chymostatin
-
IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
chymostatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
chymostatin
-
IC50 at pH 5.6: 0.013 mM, IC50 at pH 6.5: 0.0022 mM
chymostatin
-
1 mM, 89% inhibition
chymostatin
-
1 mM, 36% inhibition, isoenzyme MpiCP-1
chymostatin
-
5% residual activity at 1 mM
CoSO4
-
62% residual activity at 10 mM
CuCl
-
1 mM, 37% inhibition
CuCl2
-
1 mM, 39% inhibition
CuSO4
-
4% residual activity at 10 mM
D-Amino acids
-
less inhibitory than the L-enantiomers, non-competitive or mixed-type
D-Phe ethyl ester
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
Citrus sp.
-
peel enzyme inhibited, leaf enzyme not
diisopropyl fluorophosphate
-
benzyloxycarbonyl-L-phenylalanyl chloromethane-inhibited enzyme does not react with the inhibitor
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
effective inhibitor
diisopropylfluorophosphate
-
1 mM, 63% inhibition
diisopropylfluorophosphate
-
1 mM, 39% inhibition, isoenzyme MpiCP-1; 1 mM, 67% inhibition, isoenzyme MpiCP-2
diisopropylfluorophosphate
-
complete inhibition at 5 mM, at 30C and pH 3.1
dimethylformamide
-
-
E-64
-
1 mM, 10% inhibition, isoenzyme MpiCP-2; 1 mM, 22% inhibition, isoenzyme MpiCP-1
ebelactone B
-
IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
ebelactone B
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
ebelactone B
-
IC50: 0.0021 mM (at pH 5.6), IC50: 0.0015 mM (at pH 6.5)
EDTA
-
1 mM, 38% inhibition, isoenzyme MpiCP-1
Elastatinal
-
1 mM, 46% inhibition, isoenzyme MpiCP-2
ethanol
Citrus sp.
-
above 5%
FeCl3
-
1 mM, 92% inhibition
HgCl2
-
1 mM, 54% inhibition
HgCl2
-
complete inhibition at 1 mM, at 30C and pH 3.1
iodoacetamide
-
slight
L-amino acids
-
competitive
lactacystin
-
IC50 at pH 5.6: 0.0052 mM, IC50 at pH 6.5: 0.0018 mM
lactacystin
-
IC50 at pH 5.6: 0.048 mM, IC50 at pH 6.5: 0.031 mM
lactacystin
-
IC50 at pH 5.6: 0.0014 mM, IC50 at pH 6.5: 0.0043 mM
lactacystin
-
CatA is inhibited by 0.03 mM lactacystin
Leupeptin
-
1 mM, 24% inhibition, isoenzyme MpiCP-1; 1 mM, 60% inhibition, isoenzyme MpiCP-2
MnCl2
-
1 mM, 14% inhibition
Monoiodoacetic acid
-
1 mM, 14% inhibition; 1 mM, 25% inhibition
N-(N-[1-trans-3-carboxyoxiran-2-carbonyl]-L-leucyl)-agmatine
-
93% residual activity at 1 mM
Nalpha-tosyl-L-Lys-chloromethyl ketone
-
1 mM, 13% inhibition
Nalpha-tosyl-L-Lys-chloromethyl ketone
-
1 mM, 13% inhibition, isoenzyme MpiCP-2
Nalpha-tosyl-L-Phe-chloromethyl ketone
-
1 mM, 57% inhibition
-
Nalpha-tosyl-L-Phe-chloromethyl ketone
-
1 mM, 12% inhibition, isoenzyme MpiCP-2
-
NEM
-
1 mM, 71% inhibition
NH2-blocked amino acids
-
-
-
omuralide
-
might inhibit cathepsin A at the S1 subsite in the active-site cleft through direct binding to the active serine residue
omuralide
-
IC50 at pH 5.6: 0.000099 mM, IC50 at pH 6.5: 0.000012 mM
omuralide
-
IC50 at pH 5.6: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
omuralide
-
IC50 at pH 5.6: 0.0000048 mM, IC50 at pH 6.5: 0.000002 mM
p-chloromercuribenzenesulfonate
-
-
p-chloromercuribenzoic acid
-
complete inhibition at 1 mM, at 30C 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
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
mercurials inhibit the hydrolysis of the good substrate benzyloxycarbonyl-L-Phe-L-Leu, the inhibition is repressed by the competitive inhibitors benzyloxycarbonyl-D-Phe-D-Leu-Leu-Phe, trans-cinnamate and acetyl-D-Phe ethyl ester. Aromatic, methyl and ethyl mercurials do not cause complete inactivation with the poor substrates benzyloxycarbonyl-Gly-Phe and benzoyl-Gly-beta,L-phenyllactate. Propyl and butyl-mercurials enhance these activities
Pb(CH3COO)2
-
60% residual activity at 10 mM
PbCl2
-
1 mM, 95% inhibition
PCMB
-
1 mM, 95% inhibition
PCMB
-
1 mM, 28% inhibition, isoenzyme MpiCP-1; 1 mM, 97% inhibition, isoenzyme MpiCP-2
pepstatin A
-
1 mM, 8% inhibition
pepstatin A
-
1 mM, 11% inhibition, isoenzyme MpiCP-2; 1 mM, 19% inhibition, isoenzyme MpiCP-1
Phe-Asn-Arg-Ala-Val-Asp
-
-
Phe-Asn-Arg-Ala-Val-Val
-
-
Phe-Asn-Arg-Pro-Val-Asp
-
-
Phe-Asn-Arg-Pro-Val-Val
-
-
Phe-ethyl ester
-
-
phenylmethane sulfonylfluoride
-
-
phenylmethylsulfonyl fluoride
-
irreversible
Phenylmethylsulfonylfluoride
-
1 mM, 72% inhibition
Phenylmethylsulfonylfluoride
-
1 mM, 61% inhibition, isoenzyme MpiCP-1; 1 mM, complete inhibition, isoenzyme MpiCP-2
Phenylmethylsulfonylfluoride
-
48% residual activity at 1 mM
phosphoramidon
-
1 mM, 17% inhibition, isoenzyme MpiCP-1; 1 mM, 41% inhibition, isoenzyme MpiCP-2
piperastatin A
-
IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
piperastatin A
-
IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 mM
piperastatin A
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
piperastatin A
-
1 mM, 70% inhibition
piperastatin A
-
1 mM, 17% inhibition, isoenzyme MpiCP-2; 1 mM, 87% inhibition, isoenzyme MpiCP-1
poly-L-lysine
-
-
poststatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
poststatin
-
IC50 at pH 5.6: 0.089 mM, IC50 at pH 6.5: 0.029 mM
poststatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
Product analogs
-
-
-
SDS
-
1 mM, complete inhibition
SnCl2
-
1 mM, complete inhibition
Substrate analogs
-
-
-
Tfs1p
-
NatB-dependent acetylation is essential for the inhibitory activity on carboxypeptidase Y
-
tosylphenylalanylchloromethane
-
1 mM, 35% inhibition, isoenzyme MpiCP-1
trans-epoxysuccinyl-L-leucylamido-(4-guanidine)-butane
-
-
ZnSO4
-
69% residual activity at 10 mM
Monoiodoacetic acid
-
complete inhibition at 1 mM, at 30C and pH 3.1
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
Citrus sp.
-
not inhibition by EDTA
-
additional information
-
studies on the carboxypeptidase Y-inhibitor complex of yeast
-
additional information
-
no inhibition with 1 mM EDTA or chymostatin
-
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
-
not inhibited by trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
additional information
-
not inhibited by ICh, a homolog of carboxypeptidase inhibitor IC
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-chloro-3-tosylamido-2-heptanone
-
10% increase of activity at 10 mM
3-Phenyl-1-propanol
-
inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe
antipain
-
15 increase of activity at 0.1 mM
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
EDTA
-
25% increase of activity at 10 mM
N-ethylmaleimide
-
8% increase of activity at 10 mM
o-phenanthroline
-
4% increase of activity at 5 mM
pepstatin A
-
5% increase of activity at 0.1 mM
proteinase A
-
active proteinase A is essential to the activity of carboxypeptidase Y
-
proteinase K
-
converts the proenzyme to the mature, active enzyme
-
Leupeptin
-
20% increase of activity at 0.1 mM
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
-
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
-
-
0.0082
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
0.024
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
0.035
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
0.21
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
0.0024
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 5.0
0.009
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 6.5
0.00059
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
0.0025
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
0.0001
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
0.00013
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
0.0001
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
0.00012
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
0.61
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
1.2
acetyl-Phe ethyl ester
-
pH 8.0, 25C
1.28
acetyl-Phe ethyl ester
-
pH 6.5, 25C
0.74
Acetyl-Phe-Leu
-
pH 6.5, 25C
2.4
Acetyl-Tyr-ethyl ester
-
-
2.4
Acetyl-Tyr-ethyl ester
-
pH 8.0, 25C
0.07
benzoyl-Ala benzyl ester
-
pH 7.5
14
benzoyl-Ala-OGly
-
pH 6.5
6.3
benzoyl-Ala-OMe
-
pH 7.5
1.7
benzoyl-Gly benzyl ester
-
pH 7.5
10
benzoyl-Gly-Arg
-
pH 6.5, 25C
0.45
benzoyl-Gly-beta-phenyllactate
-
pH 6.0, 25C
21
benzoyl-Gly-OEt
-
pH 7.5
56
benzoyl-Gly-OGly
-
pH 6.5
48
benzoyl-Gly-OMe
-
pH 7.5
0.05
benzoyl-Gly-OPhe
-
pH 6.5
7.7
benzoyl-Gly-Phe
-
pH 6.5, 25C
1.1
benzoyl-Phe-Gly
-
pH 6.5
2.4
benzoyl-Phe-OGly
-
pH 6.5
0.18
benzoyl-Phe-OMe
-
pH 7.5
0.13
benzoyl-Tyr-p-nitroanilide
-
-
3.26
Benzyloxycarbonyl-Ala-Ala
-
pH 6.5, 25C
0.57
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341G
0.98
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341F
1.1
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, wild-type enzyme anf mutant enzyme C341V
4.2
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341S
4
benzyloxycarbonyl-Arg-Pro
Citrus sp.
-
orange peel
0.053
benzyloxycarbonyl-Glu-Phe
-
pH 6.5, 25C
0.13
benzyloxycarbonyl-Glu-Phe
-
pH 5.5, 25C
3.3
benzyloxycarbonyl-Glu-Phe
-
pH 6.5, 25C
0.14
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.0, 25C
0.5
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.5, 25C
3
Benzyloxycarbonyl-Glu-Tyr
-
pH 6.0, 25C
1.15
Benzyloxycarbonyl-Gly-Glu
-
pH 4.5, 25C
9.09
Benzyloxycarbonyl-Gly-Glu
-
pH 5.5, 25C
1.75
benzyloxycarbonyl-Gly-Gly
-
pH 6.5, 25C
0.83
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, wild-type enzyme
0.89
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341V
3.2
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341G
5.2
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341S
8.4
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341F
9.1
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341D
0.41
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, wild-type enzyme
0.45
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341V
1.7
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C
3.7
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341G
6.7
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341S
19
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341F
0.1
Benzyloxycarbonyl-His-Phe
-
pH 6.5, 25C
0.23
Benzyloxycarbonyl-His-Phe
-
pH 7.0, 25C
0.38
Benzyloxycarbonyl-His-Phe
-
pH 7.5, 25C
0.83
benzyloxycarbonyl-His-Tyr
-
pH 5.7, 25C
1.33
benzyloxycarbonyl-His-Tyr
-
pH 6.5, 25C
1.82
benzyloxycarbonyl-His-Tyr
-
pH 7.5, 25C
0.068
benzyloxycarbonyl-Leu-Leu
-
pH 6.5, 25C
0.1
benzyloxycarbonyl-Leu-Phe
-
pH 6.5, 25C
0.5
benzyloxycarbonyl-Leu-Phe
Citrus sp.
-
orange peel
0.5
benzyloxycarbonyl-Leu-Phe
-
benzyloxycarbonyl-Phe-Phe at pH 6.5
0.5
benzyloxycarbonyl-Leu-Phe
-
pH 6.5, 25C
0.56
benzyloxycarbonyl-Phe-Ala
-
pH 6.5, 25C
9
benzyloxycarbonyl-Phe-beta-Ala
-
pH 6.5, 25C
-
0.36
benzyloxycarbonyl-Phe-Glu
-
pH 4.5, 25C
0.41
benzyloxycarbonyl-Phe-Glu
-
furylacryloyl-Phe-Gly-OH
0.41
benzyloxycarbonyl-Phe-Glu
-
pH 5.5, 25C
16.5
benzyloxycarbonyl-Phe-Glu
-
pH 6.5, 25C
4
benzyloxycarbonyl-Phe-Gly
-
pH 6.5, 25C
-
4
benzyloxycarbonyl-Phe-Gly
-
pH 6.5
-
0.9
benzyloxycarbonyl-Phe-His
-
pH 5.5, 25C
-
3.2
benzyloxycarbonyl-Phe-His
-
pH 6.5, 25C
-
0.07
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341F
0.1
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C
0.16
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341V
0.19
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, wild-type enzyme
0.24
Benzyloxycarbonyl-Phe-Leu
-
pH 6.0, 25C
0.26
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341G
0.32
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341S
3
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341D
10
benzyloxycarbonyl-Phe-NH2
-
pH 8.0, 25C
-
10
benzyloxycarbonyl-Phe-NH2
-
pH 8.0
-
11
benzyloxycarbonyl-Phe-NH2
-
pH 7.0, 25C
-
15
benzyloxycarbonyl-Phe-NH2
-
pH 6.0, 25C
-
0.67
benzyloxycarbonyl-Phe-Pro
-
pH 6.5, 25C
-
0.86
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37C
1.33
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37C, isoenzyme MpiCP-1
1.55
benzyloxycarbonyl-Tyr-Glu
-
pH 3.5, 37C, isoenzyme MpiCP-2
0.022
endothelin
-
-
-
0.075
Furylacryloyl-Phe ethyl ester
-
wild-type
0.14
furylacryloyl-Phe-Ala
-
pH 6.5
5.4
furylacryloyl-Phe-Gly
-
pH 6.5
0.021
furylacryloyl-Phe-Leu
-
pH 6.5
0.16
Furylacryloyl-Phe-OGly-OH
-
wild-type
0.39
furylacryloyl-Phe-OMe
-
pH 7.5
0.047
furylacryloyl-Phe-Val
-
pH 6.5
0.029
N-benzoyl-L-tyrosine-p-nitroanilide
-
-
0.45
Hippuryl-beta-phenyl lactate
-
-
additional information
additional information
-
overview: synthetic substrates
-
additional information
additional information
-
-
-
additional information
additional information
-
influence of mercurials
-
additional information
additional information
-
kinetic characterization of peptide semisynthesis
-
additional information
additional information
-
-
-
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
-
-
2.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
4.1
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
5.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 6.5
6.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala
-
pH 5.0
2.2
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 6.5
3.8
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala
-
pH 5.0
2.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
3.9
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
2.3
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
3.7
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
2.3
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 6.5
3.5
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala
-
pH 5.0
1777
9-[(R)-2-[[(S)-[[(S)-1-(isopropoxycarbonyl)ethyl]amino]phenoxyphosphinyl]methoxy]-propyl]adenine
-
-
120
acetyl-Phe ethyl ester
-
pH 8.0, 25C
122
acetyl-Phe ethyl ester
-
pH 6.5, 25C
36.1
Acetyl-Phe-Leu
-
pH 6.5, 25C
105
Acetyl-Tyr ethyl ester
-
-
105
Acetyl-Tyr ethyl ester
-
pH 8.0, 25C
123
benzoyl-Ala benzyl ester
-
pH 7.5
58.3
benzoyl-Ala-OGly
-
pH 6.5
51.7
benzoyl-Ala-OMe
-
pH 7.5
18.3
benzoyl-Gly benzyl ester
-
pH 7.5
1.44
benzoyl-Gly-Arg
-
pH 6.5, 25C
21.2
benzoyl-Gly-beta-phenyllactate
-
pH 6.0, 25C
2.5
benzoyl-Gly-OEt
-
pH 7.5
30
benzoyl-Gly-OGly
-
pH 6.5
2.5
benzoyl-Gly-OMe
-
pH 7.5
18.3
benzoyl-Gly-OPhe
-
pH 6.5
3.8
benzoyl-Gly-Phe
-
pH 6.5, 25C
3.83
benzoyl-Gly-Phe
-
pH 6.5
11.5
benzoyl-Phe-Gly
-
pH 6.5
35
benzoyl-Phe-OGly
-
pH 6.5
152
benzoyl-Phe-OMe
-
pH 7.5
2.1
benzoyl-Tyr-4-nitroanilide
-
-
69.4
Benzyloxycarbonyl-Ala-Ala
-
pH 6.5, 25C
465
Benzyloxycarbonyl-Ala-Leu
-
-
2.2
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341F
8
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341V
93
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341S
95
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, mutant enzyme C341G
150
Benzyloxycarbonyl-Ala-Phe
-
pH 6.5, 25C, wild-type enzyme
13.3
benzyloxycarbonyl-Glu-Phe
-
pH 6.5, 25C
15.5
benzyloxycarbonyl-Glu-Phe
-
pH 4.5, 25C
16.8
benzyloxycarbonyl-Glu-Phe
-
pH 5.5, 25C
18.8
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.0, 25C
19
Benzyloxycarbonyl-Glu-Tyr
-
pH 5.5, 25C
23.8
Benzyloxycarbonyl-Glu-Tyr
-
pH 6.0, 25C
0.32
Benzyloxycarbonyl-Gly-Glu
-
pH 4.5, 25C
0.46
Benzyloxycarbonyl-Gly-Glu
-
pH 5.5, 25C
2.18
benzyloxycarbonyl-Gly-Gly
-
pH 6.5, 25C
0.467
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341V
1.4
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341D
1.9
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341S
2.3
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341F
3.2
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, wild-type enzyme
7
Benzyloxycarbonyl-Gly-Leu
-
pH 6.5, 25C, mutant enzyme C341G
0.16
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341V
0.96
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, wild-type enzyme
1.1
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341G
2.2
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C
2.4
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341S
5.5
Benzyloxycarbonyl-Gly-Phe
-
pH 6.5, 25C, mutant enzyme C341F
0.72
Benzyloxycarbonyl-His-Phe
-
pH 6.5, 25C
1.82
Benzyloxycarbonyl-His-Phe
-
pH 7.0, 25C
2.05
Benzyloxycarbonyl-His-Phe
-
pH 7.5, 25C
8.2
benzyloxycarbonyl-His-Tyr
-
pH 6.5 or pH 7.5, 25C
10.7
benzyloxycarbonyl-His-Tyr
-
pH 5.7, 25C
6.85
benzyloxycarbonyl-Leu-Leu
-
pH 6.5, 25C
46
benzyloxycarbonyl-Leu-Phe
-
pH 6.5, 25C
120
benzyloxycarbonyl-Phe-Ala
-
pH 6.5, 25C
66
benzyloxycarbonyl-Phe-beta-Ala
-
pH 6.5, 25C
-
24.5
benzyloxycarbonyl-Phe-Glu
-
pH 4.5, 25C
26.2
benzyloxycarbonyl-Phe-Glu
-
pH 5.5, 25C
96.5
benzyloxycarbonyl-Phe-Glu
-
pH 6.5, 25C
140
benzyloxycarbonyl-Phe-Gly
-
-
-
140
benzyloxycarbonyl-Phe-Gly
-
pH 6.5, 25C
-
3
benzyloxycarbonyl-Phe-His
-
pH 5.5, 25C
-
11.6
benzyloxycarbonyl-Phe-His
-
pH 6.5, 25C
-
1.2
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341F
2.1
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341D
4.6
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341V
15
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341G
15.1
Benzyloxycarbonyl-Phe-Leu
-
pH 6.0
18
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, mutant enzyme C341S
92
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C, wild-type enzyme
130
Benzyloxycarbonyl-Phe-Leu
-
pH 6.5, 25C
2.2
benzyloxycarbonyl-Phe-NH2
-
pH 7.0, 25C
-
2.8
benzyloxycarbonyl-Phe-NH2
-
pH 6.0, 25C
-
5.3
benzyloxycarbonyl-Phe-NH2
-
pH 8.0, 25C
-
5.33
benzyloxycarbonyl-Phe-NH2
-
pH 8.0
-
420
benzyloxycarbonyl-Phe-Phe
-
-
420
benzyloxycarbonyl-Phe-Phe
-
pH 6.5, 25C
23
benzyloxycarbonyl-Phe-Pro
-
pH 6.5, 25C
-
291
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37C
723
benzyloxycarbonyl-Tyr-Glu
-
pH 4.0, 37C, isoenzyme MpiCP-1
2039
benzyloxycarbonyl-Tyr-Glu
-
pH 3.5, 37C, isoenzyme MpiCP-2
24.2
endothelin
-
-
-
68.3
Furylacryloyl-Phe ethyl ester
-
wild-type enzyme
162
furylacryloyl-Phe-Ala
-
pH 6.5
96.7
furylacryloyl-Phe-Gly
-
pH 6.5
61.7
Furylacryloyl-Phe-Gly-OH
-
wild-type enzyme
81.7
furylacryloyl-Phe-Leu
-
pH 6.5
24.2
Furylacryloyl-Phe-OGly-OH
-
wild-type enzyme
183
furylacryloyl-Phe-OMe
-
pH 7.5
108
furylacryloyl-Phe-Val
-
pH 6.5
21.2
Hippuryl-beta-phenyl lactate
-
-
additional information
additional information
-
overview: synthetic substrates
-
additional information
additional information
-
-
-
additional information
additional information
-
conformational differences reflected in kinetic behaviour in water and deuterium oxide
-
additional information
additional information
-
influence of mercurials
-
additional information
additional information
-
kinetic characterization of peptide semisynthesis
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
260
acetyl-D-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
30
acetyl-D-Phe ethyl ester
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
12
acetyl-D-Phe-ethyl ester
-
esterase activity
20
Acetyl-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
25
Acetyl-Phe
-
esterase activity
1.3
benzyloxycarbonyl-D-Phe
-
esterase activity
1.7
benzyloxycarbonyl-D-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
0.2
benzyloxycarbonyl-D-Phe-D-Leu
-
esterase activity
0.3
benzyloxycarbonyl-D-Phe-D-Leu
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
0.6
Benzyloxycarbonyl-Phe
-
esterase activity
0.7
Benzyloxycarbonyl-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
2.6
beta-phenyl-L-lactate
-
esterase activity
5.7
beta-phenyl-L-lactate
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
1.9
Beta-phenylpropionate
-
esterase activity
4.5
Beta-phenylpropionate
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
0.000021
carboxypeptidase Y inhibitor IC
-
pH 4.7, hydrolysis of
-
24
D-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
5.3
D-Phe ethyl ester
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
11
D-Phe ethyl ester
-
esterase activity
0.9
Leu-Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
2.6
Leu-Phe
-
esterase activity
0.4
Phe
-
esterase activity
3.9
Phe
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
8.3
Phe ethyl ester
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
9.1
Phe ethyl ester
-
esterase activity
3.1
trans-Cinnamate
-
esterase activity
8
trans-Cinnamate
-
hydrolysis of benzyloxycarbonyl-Phe-Leu
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0006
3,4-Dichloroisocoumarin
-
-
0.0022 - 0.013
chymostatin
-
IC50 at pH 5.6: 0.013 mM, IC50 at pH 6.5: 0.0022 mM
0.092 - 0.1
chymostatin
-
IC50 at pH 5.6: 0.092 mM, IC50 at pH 6.5: above 0.1 mM
0.1
chymostatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
0.01
diisopropyl fluorophosphate
-
-
0.00002 - 0.00003
ebelactone B
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
0.0015
ebelactone B
-
IC50: 0.0021 mM (at pH 5.6), IC50: 0.0015 mM (at pH 6.5)
0.0016 - 0.002
ebelactone B
-
IC50 at pH 5.6: 0.0016 mM, IC50 at pH 6.5: 0.002 mM
0.0014 - 0.0043
lactacystin
-
IC50 at pH 5.6: 0.0014 mM, IC50 at pH 6.5: 0.0043 mM
0.0018 - 0.0052
lactacystin
-
IC50 at pH 5.6: 0.0052 mM, IC50 at pH 6.5: 0.0018 mM
0.031 - 0.048
lactacystin
-
IC50 at pH 5.6: 0.048 mM, IC50 at pH 6.5: 0.031 mM
0.000002 - 0.0000048
omuralide
-
IC50 at pH 5.6: mM, IC50 at pH 6.5: 0.000002 mM
0.000012 - 0.000099
omuralide
-
IC50 at pH 5.6: 0.000099 mM, IC50 at pH 6.5: 0.000012 mM
0.000078 - 0.000096
omuralide
-
IC50 at pH 5.6: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
0.72
Phe-Asn-Arg-Ala-Val-Asp
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.63
Phe-Asn-Arg-Ala-Val-Val
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.91
Phe-Asn-Arg-Pro-Val-Asp
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.71
Phe-Asn-Arg-Pro-Val-Val
-
in 50 mM Tris-HCl and 0.1 M NaCl (pH 7.5)
0.0041 - 0.0045
piperastatin A
-
IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 mM
0.018 - 0.032
piperastatin A
-
IC50 at pH 5.6: 0.018 mM, IC50 at pH 6.5: 0.032 mM
0.1
piperastatin A
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
0.029 - 0.089
poststatin
-
IC50 at pH 5.6:0.089 mM, IC50 at pH 6.5: 0.029 mM
0.1
poststatin
-
IC50 at pH 5.6 and at pH 6.5: above 0.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
isoenzyme MpiCP-2
additional information
Citrus sp.
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
isoenzyme MpiCP-2
4
-
hydrolysis of benzyloxycarbonyl-Glu-Tyr
4
-
isoenzyme MpiCP-1
4.2
-
hydrolysis of polyglutamic acid
5.3 - 5.7
Citrus sp.
-
benzyloxycarbonyl-Leu-Phe, benzyloxycarbonyl-Arg-Pro, orange peel
5.3
Citrus sp.
-
-
5.5
-
or below, release of C-terminal acidic amino acids
5.5
-
peptides containing an acidic amino acid, e.g. benzyloxycarbonyl-Phe-Glu, and benzyloxycarbonyl-Glu-Phe
5.5
-
hydrolysis of furyacryloyl-Phe-Ala
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
6
-
hydrolysis of benzoyl-Gly-Arg
7
-
around, release of C-terminal basic amino acids
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
Citrus sp.
-
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
above 30C
40
Citrus sp.
-
20 min incubation, benzyloxycarbonyl-Leu-Phe
40
-
hydrolysis of benzyloxycarbonyl-Glu-Tyr
50
-
hydrolysis of furyacryloyl-Phe-Ala
50
-
isoenzyme MpiCP-1; isoenzyme MpiCP-2
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30C: about 45% of maximal activity, 55C: 75% of maximal activity, hydrolysis of furyacryloyl-Phe-Ala
30
Citrus sp.
-
30C: about 65% of activity maximum, 60C: about 70% of activity maximum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.7
-
isoenzyme MpiCP-1
4
-
isoenzyme MpiCP-2
4.5
Citrus sp.
-
orange leaf
5.5
-
isoelectric focusing
6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
nerve fiber
Manually annotated by BRENDA team
-
expressed in Escherichia coli
Manually annotated by BRENDA team
-
Carlbiotech, Copenhagen, Denmark, wild type and mutant enzyme
Manually annotated by BRENDA team
-
from Peptech, Hilleroed, Denmark
Manually annotated by BRENDA team
-
of digestive tract
Manually annotated by BRENDA team
-
SmSCP-1 is nearly 2fold in female fat body compared to male fat body
Manually annotated by BRENDA team
-
from a galactosialidosis patient transformed with simian virus-40-adenovirus recombinant
Manually annotated by BRENDA team
Citrus sp.
-
flavedo
Manually annotated by BRENDA team
-
nerve fiber
Manually annotated by BRENDA team
-
embryonic
Manually annotated by BRENDA team
-
Scpep 1 is restricted to proximal convoluted tubular epithelium
Manually annotated by BRENDA team
Citrus sp.
-
-
Manually annotated by BRENDA team
-
macrophage-like cells
Manually annotated by BRENDA team
P16675
a cDNA of bone marrow-derived monocyte/macrophage osteoclast progenitors is used
Manually annotated by BRENDA team
Citrus sp.
-
flavedo
Manually annotated by BRENDA team
-
macrophage-like cells
Manually annotated by BRENDA team
-
Leydig cells
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
P16675
small amount also present in cytosolic fraction of transfected HEK-293 cells
Manually annotated by BRENDA team
Q6Y3Z8
membrane bound compartments between nucleus and kinetoplast
-
Manually annotated by BRENDA team
Trypanosoma cruzi Y
-
membrane bound compartments between nucleus and kinetoplast
-
-
Manually annotated by BRENDA team
-
recombinant enzyme expressed in Escherichia coli
Manually annotated by BRENDA team
P16675
in transfected HEK-293 cells
Manually annotated by BRENDA team
Trypanosoma cruzi Y
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
the localization determinant resides in the propeptide of the enzyme
Manually annotated by BRENDA team
-
vacuolar storage protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
-
SDS-PAGE
677595
32000
-
mature enzyme, SDS-PAGE
702451
32000
-
mature form, SDS-PAGE
703982
32000
-
mature enzyme, SDS-PAGE
704549
36000
-
SDS-PAGE
679935
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
680325
42000
-
gel filtration
679935
50000
-
proform, SDS-PAGE
703982
54000
-
proenzyme, SDS-PAGE
702451
55000
Q920A5
SDS-PAGE
708470
60000
-
-
647206
61000
-
-
647189
61000
-
sedimentation equilibrium measurement
647195
61000
-
mature enzyme, SDS-PAGE
680774
67000
-
gel filtration
665235
70000
-
proenzyme, SDS-PAGE
702764
86000
Citrus sp.
-
enzyme from peel, gel filtration
647194
100000
-
native complex, SDS-PAGE
677595
125000
-
isoenzyme MpiCP-1, gel filtration
665932
126000
Citrus sp.
-
enzyme from peel, gel filtration
647211
132000
-
gel filtration
665930
135000
-
SDS-PAGE
682319
150000
-
SDS-PAGE
680306
175000
Citrus sp.
-
enzyme from leaf, gel filtration
647194, 647211
additional information
-
nucleotide sequence
647204
additional information
Citrus sp., Homo sapiens
-
overview
647222
additional information
-
-
647222
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 61000, SDS-PAGE
?
-
x * 47000, recombinant enzyme, SDS-PAGE
dimer
-
1 * 64000 + 1 * 67000, SDS-PAGE
dimer
-
2 * 61000, isoenzyme MpiCP-1, SDS-PAGE
homotrimer
-
3 * 50000, SDS-PAGE
oligomer
-
38 * 59000, isoenzyme MpiCP-2, SDS-PAGE
trimer
-
3 * 45000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE, 1 * 42000, gel filtration
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
additional information
Q920A5
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
Citrus sp., Homo sapiens
-
-
glycoprotein
-
11% carbohydrate, isoenzyme MpiCP-1, 33% carbohydrate, isoenzyme MpiCP-2
glycoprotein
-
contains 17% carbohydrate
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
proteolytic modification
-
structural integrity and functional activity is influenced by its associated carbohydrate component
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
glycoprotein
Saccharomyces cerevisiae EOS1
-
-
-
glycoprotein
-
-
proteolytic modification
-
Scpep1 is proteolytically cleaved to a mature enzyme
additional information
-
fusion with the N-terminal half of the Zea mays prolamin gamma-zein forms endoplasmic reticulum-located protein bodies
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Citrus sp., Homo sapiens
-
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
-
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
-
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 30C for 30 min
679935
2 - 8
-
37C, 1 h, stable
665930
2 - 8
-
37C, 1 h, isoenzyme MpiCP-1 is stable
665932
3
-
quick loss of activity below
647189, 647195
4 - 6
Citrus sp.
-
orange leaf enzyme is unstable below pH 4 and above pH 6; stable, irreversible inactivation above pH 6, orange peel
647194
4 - 6
Citrus sp.
-
orange leaf enzyme is unstable below pH 4 and above pH 6
647211
5
Citrus sp.
-
most stable at, orange leaf enzyme
647194
5
Citrus sp.
-
most stable at room temperature
647211
5.5 - 6.6
-
37C, 1 h, isoenzyme MpiCP-2 is stable up to
665932
5.5 - 8
-
8 h, 25C, stable
647189, 647195
5.5
-
somewhat unstable above at 37C
647190
6 - 8
-
37C, stable for 2 h
647195
6 - 9
-
stable
665235
7
-
at temperatures above 25C the enzyme is most stable at pH 7.0
647189, 647195
additional information
-
rapid and irreversible inactivation at low pH
647206
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-30 - 20
-
30 min, 0.1 mPa, nearly full activity is maintained
647230
10
-
400 mPa, 10 min, 50% loss of activity
647230
25
-
pH 5.5-8, stable
647189
37
-
pH 6-8, stable for 2 h
647195
45 - 50
-
the enzyme activity remained intact at temperatures below 45C, but declined rapidly at temperatures exceeding 50C
679935
50
-
pH 5.0, 15 min, stable up to
665930
50
-
pH 6.0, 15 min, isoenzyme MpiCP-2 is stable up to
665932
55
-
unstable above
665235
55
-
pH 6.0, 15 min, isoenzyme MpiCP-1 is stable
665932
60
-
quick loss of activity above
647189, 647195
additional information
-
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5C, 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
647230
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
citrus peel enzyme is inactivated upon lyophilization
Citrus sp.
-
orange leaf enzyme is stable to lyophilization
Citrus sp.
-
orange peel enzyme is inactivated upon lyophilization
Citrus sp.
-
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
-
urea, 6 M, about 80% of activity is retained after 1 h
-
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5C, 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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-chloroethanol
-
10% stable at pH 7.0 for at least 15 min
dioxane
-
30% stable at pH 7.0 for at least 15 min
Ethylene glycol
-
60% stable at pH 7.0 for at least 15 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 4.7-5.5, stable for several months
Citrus sp.
-
4C, pH 4.7-5.5, stable for a few days
Citrus sp.
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Citrus sp.
-
Superdex S-200 gel filtration and HR Mono P column chromatography
-
TSK-DEAE 5PW column chromatography
-
isoenzyme MpiCP-1; isoenzyme MpiCP-2
-
-
Q920A5
anti-FLAG affinity column chromatography
-
Butyl-Toyopearl 650C column chromatography and DEAE Sephadex A-50 gel filtration
-
development of a novel method that can produce active yeast enzyme from inactive inclusion bodies expressed in escherichia coli
-
wild-type and mutant enzymes
-
Mono S cation exchange column chromatography and Superdex 75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in insect cells
-
expressed in Pichia pastoris
-
expressed in T-1 cells
-
expressed in HEK293 cells
P16675
expressed in HT-1080 cells
Q920A5
expressed in Arabidopsis thaliana
-
expressed in Nicotiana tabacum as a fusion protein
-
expressed in Saccharomyces cerevisiae strain BJ2168
-
expression in Escherichia coli. The native enzyme is a glycoprotein whereas the recombinant enzyme produced from Escherichia coli is not glycosylated
-
ENGINEERING
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
R344A
-
the mutant shows about wild type cathepsin A activity
R344D
-
inactive mutant, the 54 kDa precursor/zymogen with the R344D substitution is not processed to the 32/20 kDa mature form with CathA activity
R344E
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344G
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344I
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344K
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344M
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344N
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344P
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344Q
-
the mutant shows reduced cathepsin A activity compared to the wild type
R344S
-
the mutant shows about wild type cathepsin A activity
R344V
-
the mutant shows reduced cathepsin A activity compared to the wild type
T343F
-
the mutant accumulates in the microsomal fraction of protoplasts treated with 2-mercaptoethanol and is for the most part susceptible to digestion by endoglycosidase H
C341F
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
C341G
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu and benzyloxycarbonyl-Gly-Phe, somewhat increased ratio with benzyloxycarbonyl-Ala-Phe
C341S
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
C341V
-
reduced ratio of turnover number to Km-value for the mutant enzyme compared to wild-type enzyme with the substrates benzyloxycarbonyl-Gly-Leu, benzyloxycarbonyl-Phe-Leu, benzyloxycarbonyl-Gly-Phe and benzyloxycarbonyl-Ala-Phe
E355A
-
no CPY secretion
E355Q
-
mutant shows moderate CPY secretion
E365A
-
mutant shows moderate CPY secretion
E369A
-
mutant shows moderate CPY secretion
E371A
-
mutant shows CPY secretion similar to the wild type
F367L
-
no CPY secretion
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
-
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
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
-
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
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
-
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
-
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
-
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
N356A
-
mutant shows CPY secretion similar to the wild type
N87I
-
mutant enzyme with reduced transport rate and reduced enzymatic activity, 30%
S297A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 39.7% for furylacryloyl-Ala-Leu, 161% for furylacryloyl-Ala-Glu, 66% for furylacryloyl-Ala-Lys, 80% for furylacryloyl-Ala-Arg, 126% for furylacryloyl-Phe-Ala, 109% for furylacryloyl-Phe-Val and 88.6% for furylacryloyl-Phe-Leu
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
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
-
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
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
-
-
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
Y361F
-
no CPY secretion
nutrition
-
the enzyme can be used to eliminate the bitterness of bitter peptides
additional information
-
the gene vps4 null mutant missorts the vacuolar enzyme carboxypeptidase Y
W382A
-
the mutant shows decreased activity compared to the wild type cathepsin A
additional information
P16675
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
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
additional information
-
carboxypeptidase Y is partially missorted to the cell surface in certain mutants of the COPIB subcomplex (COPIb, Sec27, Sec28, and possibly Sec33), which indicates an impairment in endosomal transport
additional information
-
the gene vps4 null mutant missorts the vacuolar enzyme carboxypeptidase Y
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
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
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