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Information on EC 3.4.16.5 - carboxypeptidase C and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00729
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3.4.16.5 carboxypeptidase CSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
carboxypeptidase y, cathepsin a, catha, deamidase, serine carboxypeptidase, protective protein/cathepsin a, scpep1, procpy, carboxypeptidase yscy, carboxypeptidase-y, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase Y
carboxypeptidase YSCY
-
-
-
-
cathepsin A
-
-
-
-
CP-MI
-
-
-
-
CP-MIII
-
-
-
-
CP-WIII
-
-
-
-
CPY
deamidase
-
-
-
-
lysosomal carboxypeptidase A
-
-
-
-
lysosomal protective protein
-
-
-
-
MO54
-
-
-
-
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
carboxypeptidase Y
-
-
-
-
carboxypeptidase Y
-
-
CPY
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9046-67-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-L-phenylalanyl-L-leucine + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
?
Glu-Asp-Glu-Phe-Phe-Leu-Ala + H2O
Glu-Asp-Glu-Phe-Phe-Leu + Ala
-
-
-
?
N-((S)-5-amino-5-(carbamoyl)pentyl)-3-(aminooxymethyl)benzamide + H2O
?
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu + Ala
-
-
-
-
?
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu-Ala + H2O
9-fluorenylmethoxycarbonyl-Glu-Glu-Glu-Glu-Glu-Glu + Ala
-
-
-
-
?
benzoyl-L-tyrosine-p-nitroanilide + H2O
benzoyl-L-tyrosine + p-nitroaniline
-
-
-
-
?
benzoyl-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala + H2O
benzyloxycarbonyl-Ala + Ala
-
-
-
-
?
Benzyloxycarbonyl-Ala-Leu + H2O
Benzyloxycarbonyl-Ala + Leu
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
-
-
-
-
?
benzyloxycarbonyl-Glu-Leu + H2O
benzyloxycarbonyl-Glu + Leu
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
benzyloxycarbonyl-Glu + Phe
-
-
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
-
-
-
?
benzyloxycarbonyl-Gly-Arg + H2O
benzyloxycarbonyl-Gly + Arg
-
-
-
-
?
benzyloxycarbonyl-Gly-Glu + H2O
benzyloxycarbonyl-Gly + Glu
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Phe + H2O
benzyloxycarbonyl-Gly-Gly + Phe
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro + H2O
benzyloxycarbonyl-Gly + Pro
-
-
-
-
?
benzyloxycarbonyl-His-Leu + H2O
benzyloxycarbonyl-His + Leu
-
-
-
-
?
benzyloxycarbonyl-His-Phe + H2O
benzyloxycarbonyl-His + Phe
-
-
-
-
?
benzyloxycarbonyl-His-Tyr + H2O
benzyloxycarbonyl-His + Tyr
-
-
-
-
?
benzyloxycarbonyl-Ile-Leu + H2O
benzyloxycarbonyl-Ile + Leu
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu + H2O
benzyloxycarbonyl-Leu + Leu
-
-
-
-
?
benzyloxycarbonyl-Leu-Phe + H2O
benzyloxycarbonyl-Leu + Phe
-
-
-
-
?
benzyloxycarbonyl-Nle-Leu + H2O
benzyloxycarbonyl-Nle + Leu
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala + H2O
benzyloxycarbonyl-Phe + Ala
-
-
-
-
?
benzyloxycarbonyl-Phe-beta-Ala + H2O
benzyloxycarbonyl-Phe + beta-Ala
-
-
-
-
?
benzyloxycarbonyl-Phe-Glu + H2O
benzyloxycarbonyl-Phe + Glu
-
-
-
-
?
benzyloxycarbonyl-Phe-Gly + H2O
benzyloxycarbonyl-Phe + Gly
-
-
-
-
?
benzyloxycarbonyl-Phe-His + H2O
benzyloxycarbonyl-Phe + His
-
-
-
-
?
benzyloxycarbonyl-Phe-Phe + H2O
benzyloxycarbonyl-Phe + Phe
-
-
-
-
?
benzyloxycarbonyl-Phe-Pro + H2O
benzyloxycarbonyl-Phe + Pro
-
-
-
-
?
benzyloxycarbonyl-Pro-Leu + H2O
benzyloxycarbonyl-Pro + Leu
-
-
-
-
?
benzyloxycarbonyl-Ser-Leu + H2O
benzyloxycarbonyl-Ser + Leu
-
-
-
-
?
benzyloxycarbonyl-Val-Leu + H2O
benzyloxycarbonyl-Val + Leu
-
-
-
-
?
endothelin I + H2O
endothelin(1-20) + Trp
-
containing the hydrophobic sequence Ile19-Ile20-Trp21-OH
-
?
furylacryloyl-Phe-Ala + H2O
furylacryloyl-Phe + Ala
-
-
-
-
?
furylacryloyl-Phe-Leu + H2O
furylacryloyl-Phe + Leu
-
-
-
-
?
furylacryloyl-Phe-Val + H2O
furylacryloyl-Phe + Val
-
-
-
-
?
N-(2-furanacryloyl)-Phe-Phe + H2O
N-(2-furanacryloyl)-Phe + Phe
-
-
-
-
?
N-benzoyl-L-tyrosine-p-nitroanilide + H2O
N-benzoyl-L-tyrosine + p-nitroaniline
-
-
-
-
?
pancreatic carboxypeptidase A + H2O
hydrolyzed carboxypeptidase A + C-terminal amino acid
-
-
-
?
pancreatic carboxypeptidase B + H2O
hydrolyzed pancreatic carboxypeptidase B + C-terminal amino acid
-
-
-
?
succinyl-L-Ile-L-Ile-L-Trp-7-amido-4-methylcoumarin + H2O
succinyl-L-Ile-L-Ile-L-Trp + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-Tyr + 4-nitroaniline
-
-
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
-
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
poor substrate
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
-
-
-
?
additional information
?
-
-
no effect on the activity of malate dehydrogenase
-
-
?
additional information
?
-
-
activity towards substrates with basic P1 amino acid residues is drastically increased by mutational replacement of Leu178
-
-
?
additional information
?
-
-
structural requirements for nucleophilic substrates
-
-
?
additional information
?
-
-
the mechanism involves a charge-relay system in the hydrolysis of peptide and ester substrates
-
-
?
additional information
?
-
-
inactivation of phosphoribosyltransferase
-
-
?
additional information
?
-
-
catalytic mechanism specificity overview
-
-
?
additional information
?
-
-
Asn51 and Glu145 of carboxypeptidase Y each donate a hydrogen bond to the alpha-carboxylate of peptide substrates. The same groups are involved in the interaction with the C-terminal carboxamide group of peptide amides. Asn51 donates a hydrogen bond to the C=O group of the substrate, and Glu145 (in the charged form) accepts one from the NH2 group of the substrate
-
-
?
additional information
?
-
-
mechanism of carboxypeptidase-Y-catalyzed peptide semisynthesis
-
-
?
additional information
?
-
-
endopeptidase activity is due to the presence of contaminating amounts of yeast proteinase A and caution should by taken when employing carboxypeptidase Y preparations for sequence studies
-
-
?
additional information
?
-
-
the enzyme is involved in the C-terminal processing of peptides and proteins
-
-
?
additional information
?
-
-
the enzyme is involved in the degradation of biologically active peptide amides
-
-
?
additional information
?
-
-
at semipermissive temperatures, carboxypeptidase Y transit time to the vacuole is slower in Sec- cells containing an ire1DELTA or hac1DELTA mutation than in Sec- cells with an intact unfolded protein response pathway
-
-
?
additional information
?
-
-
CPD-Y can be used to specifically modify the C-terminus of peptides and proteins, for example biotinylation of antibodies at their C-termini
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme does not require metals for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Phenyl-1-propanol
-
inhibits hydrolysis of benzyloxycarbonyl-Phe-Leu, activates hydrolysis of benzyloxycarbonyl-Gly-Phe
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
ebelactone B
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
omuralide
-
IC50 at pH 5.6: 0.000096 mM, IC50 at pH 6.5: 0.000078 mM
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
piperastatin A
-
IC50 at pH 5.6: 0.0041 mM, IC50 at pH 6.5: 0.0045 mM
Tfs1p
-
NatB-dependent acetylation is essential for the inhibitory activity on carboxypeptidase Y
-
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
-
benzyloxycarbonyl-L-phenylalanine chloromethyl ketone
-
irreversible inhibition of peptidase and esterase activity, inhibition is retarded by the competitive inhibitors benzyloxycarbonyl-D-phenylalanine-D-leucine and trans-cinnamate
diisopropyl fluorophosphate
-
benzyloxycarbonyl-L-phenylalanyl chloromethane-inhibited enzyme does not react with the inhibitor
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
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002 - 0.00003
ebelactone B
Saccharomyces cerevisiae
-
IC50 at pH 5.6: 0.00002 mM, IC50 at pH 6.5: 0.00003 mM
0.031 - 0.048
lactacystin
Saccharomyces cerevisiae
-
IC50 at pH 5.6: 0.048 mM, IC50 at pH 6.5: 0.031 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
0.029 - 0.089
poststatin
Saccharomyces cerevisiae
-
IC50 at pH 5.6:0.089 mM, IC50 at pH 6.5: 0.029 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme expressed in Escherichia coli
-
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
-
the localization determinant resides in the propeptide of the enzyme
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
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
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, crystal strcuture of the carboxypeptidase Y inhibitor Ic in complex with carboxypeptidase Y at 2.7 A resolution
carboxypeptidase Y inhibitor IC complexed with carboxypeptidase Y, hanging-drop vapour-diffusion method
-
significance of Thr60 and Met398 in hydrolysis and aminolysis reactions
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
G255R
-
PNGase releases N-glycans from the mutant during the endoplasmic reticulum-associated degradation process in vivo. A major endoproteolytic reaction on the mutant appears to occur between amino acid 400 and 404
L267A
-
kcat/Km of mutant enzyme in% of the of the wild-type value: 18.7% for furylacryloyl-Ala-Leu, 71.7% for furylacryloyl-Ala-Glu, 113% for furylacryloyl-Ala-Lys, 130% for furylacryloyl-Ala-Arg,10.8% for furylacryloyl-Phe-Ala, 18.5% for furylacryloyl-Phe-Val and 31.3% for furylacryloyl-Phe-Leu
L267D
-
mutation greatly reduces the activity towards hydrophobic P1' residues and increases the activity for the hydrolysis of substrates with Lys or Arg in P1'
L267D/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%
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
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
-
carboxypeptidase Y is partially missorted to the cell surface in certain mutants of the COPIB subcomplex (COPIb, Sec27, Sec28, and possibly Sec33), which indicates an impairment in endosomal transport
additional information
-
the gene vps4 null mutant missorts the vacuolar enzyme carboxypeptidase Y
additional information
-
three signal sequences of Saccharomyces cerevisiae mating factor a (MFalpha) and invertase (SUC2), and Kluyveromyces marxianus inulinase (INU1) are combined with proCPY to increase a transporting efficiency from the endoplasmic reticulum in Saccharomyces cerevisiae. The MFalpha signal sequence gives the best specific activity of extracellular CPY
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
at temperatures above 25°C 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
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
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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
-
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
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
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
analysis
-
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
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VOL.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Inactivation of yeast enzymes by proteinase A and B and carboxypeptidase Y from yeast
Hoppe-Seyler's Z. Physiol. Chem.
357
735-740
1976
Saccharomyces cerevisiae
Hayashi, R.
Carboxypeptidase Y in sequence determination of peptides
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1977
Saccharomyces cerevisiae
Valls, L.A.; Hunter, C.P.; Rothman, J.H.; Stevens, T.H.
Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide
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Remington, S.J.; Breddam, K.
Carboxypeptidases C and D
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Aspergillus niger, Saccharomyces cerevisiae, Triticum aestivum, Aspergillus niger CDP-AI
Hayashi, R.
Carboxypeptidase Y
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45
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Saccharomyces cerevisiae
Winther, J.R.; Sorensen, P.; Kielland-Brandt, M.C.
Refolding of a carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion
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269
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Saccharomyces cerevisiae
Sorensen, S.B.; Raaschou-Nielsen, M.; Mortensen, U.H.; Remington, S.J.; Breddam, K.
Site-directed mutagenesis on (Serine) carboxypeptidase Y from Yeast. The significance of Thr60 and Met398 in hydrolysis and aminolysis reactions.
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117
5944-5950
1995
Saccharomyces cerevisiae
-
Olesen, K.; Mortensen, U.H.; Aasmul-Olsen, S.; Kielland-Brandt, M.C.; Remington, S.J.; Breddam, K.
The activity of carboxypeptidase Y toward substrates with basic P1 amino acid residues is drastically increased by mutational replacement of leucine 178
Biochemistry
33
11121-11126
1994
Saccharomyces cerevisiae
Mortensen, U.H.; Raaschou-Nielsen, M.; Breddam, K.
Recognition of C-terminal amide groups by (serine) carboxypeptidase Y investigated by site-directed mutagenesis
J. Biol. Chem.
269
15528-15532
1994
Saccharomyces cerevisiae
Stennicke, H.R.; Mortensen, U.H.; Breddam, K.
Studies on the hydrolytic properties of (serine) carboxypeptidase Y
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35
7131-7141
1996
Saccharomyces cerevisiae
Christensen, U.
Effects of pH on carboxypeptidase-Y-catalyzed hydrolysis and aminolysis reactions
Eur. J. Biochem.
220
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1994
Saccharomyces cerevisiae
Christensen, U.; Drohse, H.B.; Molgaard, L.
Mechanism of carboxypeptidase-Y-catalysed peptide semisynthesis
Eur. J. Biochem.
210
467-473
1992
Saccharomyces cerevisiae
Lewis, W.S.; Schuster, S.M.
Structural requirements for nucleophilic substrates of carboxypeptidase Y
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266
20823-20827
1991
Saccharomyces cerevisiae
Jonson, B.A.; Aswad, D.W.
Fragmentation of isoaspartyl peptides and proteins by carboxypeptidase Y: release of isoaspartyl dipeptides as a result of internal and external cleavage
Biochemistry
29
4373-4380
1990
Saccharomyces cerevisiae
Nakagawa, Y.; Ghotb-Sharif, J.; Douglas, K.T.
Carboxypeptidase Y from Saccharomyces cerevisiae. Conformational differences reflected in kinetic behaviour in water and deuterium oxide
Biochim. Biophys. Acta
706
141-143
1982
Saccharomyces cerevisiae
Chu, F.K.; Maley, F.
Stabilization of the structure and activity of yeast carboxypeptidase Y by its high-mannose oligosaccharide chains
Arch. Biochem. Biophys.
214
134-139
1982
Saccharomyces cerevisiae
Fischer, E.P.; Holzer, H.
Interaction of proteinases and their inhibitors from yeast. Activation of carboxypeptidase Y
Biochim. Biophys. Acta
615
187-198
1980
Saccharomyces cerevisiae
Matern, H.; Barth, R.; Holzer, H.
Chemical and physical properties of the carboxypeptidase Y-inhibitor from Bakers yeast
Biochim. Biophys. Acta
567
503-510
1979
Saccharomyces cerevisiae
Lee, H.M.; Riordan, J.F.
Does carboxypeptidase Y have intrinsic endopeptidase activity?
Biochem. Biophys. Res. Commun.
85
1135-1142
1978
Saccharomyces cerevisiae
Hayashi, R.; Bai, Y.; Hata, T.
Evidence for an essential histidine in carboxypeptidase Y. Reaction with the chloromethyl ketone derivative of benzyloxycarbonyl-L-phenylalanine
J. Biol. Chem.
250
5221-5226
1975
Saccharomyces cerevisiae
Bai, Y.; Hayashi, R.
Properties of the single sulfhydryl group of carboxypeptidase Y. Effects of alkyl and aromatic mercurials on activities toward various synthetic substrates
J. Biol. Chem.
254
8473-8479
1979
Saccharomyces cerevisiae
Hayashi, R.; Bai, Y.; Hata, T.
Kinetic studies of carboxypeptidase Y. I. Kinetic parameters for the hydrolysis of synthetic substrates
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77
69-79
1975
Saccharomyces cerevisiae
Bai, Y.; Hayashi, R.; Hata, T.
Kinetic studies of carboxypeptidase Y. II. Effects of substrate and product analogs on peptidase and esterase activities
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77
81-88
1975
Saccharomyces cerevisiae
Hayashi, R.; Bai, Y.; Hata, T.
Inhibition of carboxypeptidase Y by chloromethyl ketone derivatives of benzyloxycarbonyl-L-phenylalanine
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76
1355-1357
1974
Saccharomyces cerevisiae
Barth, R.; Wolf, D.H.; Holzer, H.
Studies on the carboxypeptidase Y-inhibitor complex of yeast
Biochim. Biophys. Acta
527
63-69
1978
Saccharomyces cerevisiae
Christensen, U.
Kinetic characterization of carboxypeptidase-Y-catalyzed peptide semisynthesis prediction of yields
Amino Acids
6
177-187
1994
Saccharomyces cerevisiae
Johansen, J.T.; Breddam, K.; Ottesen, M.
Isolation of carboxypeptidase Y by affinity chromatography
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41
1-14
1976
Saccharomyces cerevisiae
-
Breddam, K.
Serine carboxypeptidases. A review
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51
83-128
1986
Saccharomyces cerevisiae, Citrus sp., Homo sapiens, Triticum aestivum
-
Mima, J.; Jung, G.; Onizuka, T.; Ueno, H.; Hayashi, R.
Amphipathic property of free thiol group contributes to an increase in the catalytic efficiency of carboxypeptidase Y
Eur. J. Biochem.
269
3220-3225
2002
Saccharomyces cerevisiae
Jung, G.; Ueno, H.; Hayashi, R.
Carboxypeptidase Y: structural basis for protein sorting and catalytic triad
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126
1-6
1999
Saccharomyces cerevisiae
Hahm, M.S.; Chung, B.H.
Refolding and purification of yeast carboxypeptidase Y expressed as inclusion bodies in Escherichia coli
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22
101-107
2001
Saccharomyces cerevisiae
Kato, M.; Sato, Y.; Shirai, K.; Hayashi, R.; Balny, C.; Lange, R.
The propeptide in the precursor form of carboxypeptidase Y ensures cooperative unfolding and the carbohydrate moiety exerts a protective effect against heat and pressure
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270
4587-4593
2003
Saccharomyces cerevisiae
Sorensen, S.B.; Breddam, K.
The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket
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6
2227-2232
1997
Saccharomyces cerevisiae
Nakase, H.; Murata, S.; Ueno, H.; Hayashi, R.
Substrate recognition mechanism of carboxypeptidase Y
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65
2465-2471
2001
Saccharomyces cerevisiae
Dumoulin, M.; Ueno, H.; Hayashi, R.; Balny, C.
Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y high pressure study
Eur. J. Biochem.
262
475-483
1999
Saccharomyces cerevisiae
Kinsho, T.; Ueno, H.; Hayashi, R.; Hashizume, C.; Kimura, K.
Sub-zero temperature inactivation of carboxypeptidase Y under high hydrostatic pressure
Eur. J. Biochem.
269
4666-4674
2002
Saccharomyces cerevisiae
Mima, J.; Hayashida, M.; Fujii, T.; Hata, Y.; Hayashi, R.; Ueda, M.
Crystallization and preliminary X-ray analysis of carboxypeptidase Y inhibitor IC complexed with the cognate proteinase
Acta Crystallogr. Sect. D
60
1622-1624
2004
Saccharomyces cerevisiae
Chang, H.J.; Jesch, S.A.; Gaspar, M.L.; Henry, S.A.
Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae
Genetics
168
1899-1913
2004
Saccharomyces cerevisiae
Satoh, Y.; Kadota, Y.; Oheda, Y.; Kuwahara, J.; Aikawa, S.; Matsuzawa, F.; Doi, H.; Aoyagi, T.; Sakuraba, H.; Itoh, K.
Microbial serine carboxypeptidase inhibitors. Comparative analysis of actions on homologous enzymes derived from man, yeast and wheat. [Erratum to document cited in CA142:109255]
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57
316-325
2004
Saccharomyces cerevisiae, Homo sapiens, Triticum aestivum
Caesar, R.; Blomberg, A.
The stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway
J. Biol. Chem.
279
38532-38543
2004
Saccharomyces cerevisiae
Mima, J.; Hayashida, M.; Fujii, T.; Narita, Y.; Hayashi, R.; Ueda, M.; Hata, Y.
Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction
J. Mol. Biol.
346
1323-1334
2005
Saccharomyces cerevisiae (P00729)
Lebed, K.; Kulik, A.J.; Forro, L.; Lekka, M.
Atomic force microscopy and quartz crystal microbalance study of the lectin-carbohydrate interaction kinetics
Acta Phys. Pol. A
111
273-286
2007
Saccharomyces cerevisiae
-
Hamberg, A.; Kempka, M.; Sjoedahl, J.; Roeraade, J.; Hult, K.
C-terminal ladder sequencing of peptides using an alternative nucleophile in carboxypeptidase Y digests
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357
167-172
2006
Saccharomyces cerevisiae
Nakamura, T.; Ando, A.; Takagi, H.; Shima, J.
EOS1, whose deletion confers sensitivity to oxidative stress, is involved in N-glycosylation in Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
353
293-298
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae EOS1
Mukherjee, S.; Kallay, L.; Brett, C.L.; Rao, R.
Mutational analysis of the intramembranous H10 loop of yeast Nhx1 reveals a critical role in ion homoeostasis and vesicle trafficking
Biochem. J.
398
97-105
2006
Saccharomyces cerevisiae
Fukada, H.; Mima, J.; Nagayama, M.; Kato, M.; Ueda, M.
Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC
Biosci. Biotechnol. Biochem.
71
472-480
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ2168
Mima, J.; Fukada, H.; Nagayama, M.; Ueda, M.
Specific membrane binding of the carboxypeptidase Y inhibitor IC, a phosphatidylethanolamine-binding protein family member
FEBS J.
273
5374-5383
2006
Saccharomyces cerevisiae
Wuenschmann, J.; Beck, A.; Meyer, L.; Letzel, T.; Grill, E.; Lendzian, K.J.
Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae
FEBS Lett.
581
1681-1687
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Lee, S.A.; Jones, J.; Khalique, Z.; Kot, J.; Alba, M.; Bernardo, S.; Seghal, A.; Wong, B.
A functional analysis of the Candida albicans homolog of Saccharomyces cerevisiae VPS4
FEMS Yeast Res.
7
973-985
2007
Candida albicans, Saccharomyces cerevisiae
Wu, T.H.; Hsieh, S.C.; Yu, C.Y.; Lee, Y.F.; Tsai, C.Y.; Yu, C.L.
Intact protein core structure is essential for protein-binding, mononuclear cell proliferating, and neutrophil phagocytosis-enhancing activities of normal human urinary Tamm-Horsfall glycoprotein
Int. Immunopharmacol.
8
90-99
2008
Saccharomyces cerevisiae
Wiradjaja, F.; Ooms, L.M.; Tahirovic, S.; Kuhne, E.; Devenish, R.J.; Munn, A.L.; Piper, R.C.; Mayinger, P.; Mitchell, C.A.
Inactivation of the phosphoinositide phosphatases Sac1p and Inp54p leads to accumulation of phosphatidylinositol 4,5-bisphosphate on vacuole membranes and vacuolar fusion defects
J. Biol. Chem.
282
16295-16307
2007
Saccharomyces cerevisiae
Franco, E.J.; Hofstetter, H.; Hofstetter, O.
A comparative evaluation of random and site-specific immobilization techniques for the preparation of antibody-based chiral stationary phases
J. Sep. Sci.
29
1458-1469
2006
Saccharomyces cerevisiae
Cabras, T.; Inzitari, R.; Fanali, C.; Scarano, E.; Patamia, M.; Sanna, M.T.; Pisano, E.; Giardina, B.; Castagnola, M.; Messana, I.
HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclization product of human salivary statherin generated by transglutaminase 2
J. Sep. Sci.
29
2600-2608
2006
Saccharomyces cerevisiae
Gabriely, G.; Kama, R.; Gerst, J.E.
Involvement of specific COPI subunits in protein sorting from the late endosome to the vacuole in yeast
Mol. Cell. Biol.
27
526-540
2007
Saccharomyces cerevisiae
Rutledge, R.M.; Ghislain, M.; Mullins, J.M.; de Thozee, C.P.; Golin, J.
Pdr5-mediated multidrug resistance requires the CPY-vacuolar sorting protein Vps3: are xenobiotic compounds routed from the vacuole to plasma membrane transporters for efflux?
Mol. Genet. Genomics
279
573-583
2008
Saccharomyces cerevisiae
Foley, D.A.; Sharpe, H.J.; Otte, S.
Membrane topology of the endoplasmic reticulum to Golgi transport factor Erv29p
Mol. Membr. Biol.
24
259-268
2007
Saccharomyces cerevisiae
Subramanian, S.; Woolford, C.A.; Drill, E.; Lu, M.; Jones, E.W.
Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast
Proc. Natl. Acad. Sci. USA
103
939-944
2006
Saccharomyces cerevisiae
Wilson, J.D.; Liu, Y.; Bentivoglio, C.M.; Barlowe, C.
Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway
Traffic
7
1213-1223
2006
Saccharomyces cerevisiae
Parr, C.L.; Keates, R.A.; Bryksa, B.C.; Ogawa, M.; Yada, R.Y.
The structure and function of Saccharomyces cerevisiae proteinase A
Yeast
24
467-480
2007
Saccharomyces cerevisiae
Peschke, B.; Bak, S.
Controlled coupling of peptides at their C-termini
Peptides
30
689-698
2009
Saccharomyces cerevisiae (P00729)
Maeda, H.; Nagayama, M.; Kuroda, K.; Ueda, M.
Purification of inactive precursor of carboxypeptidase Y using selective cleavage method coupled with molecular display
Biosci. Biotechnol. Biochem.
73
753-755
2009
Saccharomyces cerevisiae
Hosomi, A.; Suzuki, T.
Cytoplasmic peptide:N-glycanase cleaves N-glycans on a carboxypeptidase y mutant during ERAD in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1850
612-619
2015
Saccharomyces cerevisiae
Shin, S.Y.; Bae, Y.H.; Kim, S.K.; Seong, Y.J.; Choi, S.H.; Kim, K.H.; Park, Y.C.; Seo, J.H.
Effects of signal sequences and folding accessory proteins on extracellular expression of carboxypeptidase Y in recombinant Saccharomyces cerevisiae
Bioprocess Biosyst. Eng.
37
1065-1071
2014
Saccharomyces cerevisiae
Dridi, F.; Marrakchi, M.; Gargouri, M.; Saulnier, J.; Jaffrezic-Renault, N.; Lagarde, F.
Comparison of carboxypeptidase y and thermolysin for ochratoxin A electrochemical biosensing
Anal. Methods
7
8954-8960
2015
Saccharomyces cerevisiae
-
Hosomi, A.; Suzuki, T.
Cytoplasmic peptide N-glycanase cleaves N-glycans on a carboxypeptidase Y mutant during ERAD in Saccharomyces cerevisiae
Biochim. Biophys. Acta
1850
612-619
2015
Saccharomyces cerevisiae
Yu, X.; Zhai, C.; Zhong, X.; Tang, W.; Wang, X.; Yang, H.; Chen, W.; Ma, L.
High-level expression and characterization of carboxypeptidase Y from Saccharomyces cerevisiae in Pichia pastoris GS115
Biotechnol. Lett.
37
161-167
2015
Saccharomyces cerevisiae (P00729), Saccharomyces cerevisiae
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