HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.4.17.4 - Gly-Xaa carboxypeptidase
for references in articles please use BRENDA:EC3.4.17.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.4.17.4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
Gly-Xaa carboxypeptidase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-/-Leu
from yeast. In peptidase family M20, glutamate carboxypeptidase family
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9025-25-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly + H2O
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe
benzoyl-Gly-Gly + H2O
?
-
7.2% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzoyl-Gly-Lys + H2O
?
-
2% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzyloxycarbonyl-Ala-Arg(NO2) + H2O
benzyloxycarbonyl-Ala + nitroarginine
-
21% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
-
10% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
-
1.1% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzyloxycarbonyl-Gly-Glu + H2O
benzyloxycarbonyl-Gly + Glu
-
31% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzyloxycarbonyl-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly
-
13% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
-
best substrate
-
-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
-
31% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
-
1.5% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzyloxycarbonyl-Phe-Met + H2O
benzyloxycarbonyl-Phe + Met
-
1.5% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
benzyloxycarbonyl-Phe-Phe + H2O
benzyloxycarbonyl-Phe + Phe
-
1.5% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
dibenzyloxycarbonyl-Lys-Leu + H2O
dibenzyloxycarbonyl-Lys + Leu
-
5.2% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
Gly-Leu-Gly + H2O
?
-
3% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
Gly-Leu-Tyr + H2O
?
-
12% of the activity compared to benzyloxycarbonyl-Gly-Leu
-
-
?
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-Leu-Leu, benzyloxycarbonyl-Leu-Phe, dibenzyloxycarbonyl-Lys-Phe, benzyloxycarbonyl-Phe-Ser, benzyloxycarbonyl-His-Leu, benzyloxycarbonyl-Pro-Try, benzyloxycarbonyl-Gly-Gly-Leu, benzyloxycarbonyl-Gly-Gly-Phe, benzyloxycarbonyl-Gly-Leu-NH2, benzyloxycarbonyl-Gly-Phe-NH2, benzyloxycarbonyl-Ala-Phe-NH2, benzyloxycarbonyl-Phe-Leu-NH2, benzyloxycarbonyl-Phe-Leu-NH2 and Gly-Leu
-
-
-
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly + H2O
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe
-
-
enzyme assay is based on the detection of the product using HPLC to separate it from the substrate
?
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly + H2O
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe
-
-
enzyme assay is based on the detection of the product using HPLC to separate it from the substrate
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
can reverse the inhibition by chelating agents at a concentration of 0.1 mM, reactivation of 62%, inhibits the enzyme at higher concentrations, 10 mM
Mn2+
Zn2+
Mn2+
-
MnCl2, 0.1 mM and 1 mM, 106.3% and 104.2% compared to a control without additives
Zn2+
-
ZnSO4, 0.1 mM and 1 mM, 97.6% and 69.6% compared to a control without additives
Zn2+
-
can reverse the inhibition by chelating agents at a concentration of 0.1 mM, reactivation of 88%, inhibits the enzyme at higher concentrations, 10 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
irreversible inhibition, no reactivation by addition of bivalent metal ions or SH-protecting reagents like cysteine and beta-mercaptomethanol
1,10-phenanthroline
-
0.1 mM and 1 mM, 95.6% and 74.7% compared to a control without additives
1,10-phenanthroline
-
Ki: 0.035 mM, reversible by addtion of bivalent metal ions like Zn2+, Co2+, Cd2+ and Mn2+
diisopropylphosphorofluoridate
-
0.1 mM and 1 mM, 32.3% and 24.3% compared to a control without additives
EDTA
-
Ki: 0.013 mM, reversible by addtion of bivalent metal ions like Zn2+, Co2+, Cd2+ and Mn2+, Zn2+ and Co2+, at a concentration of 0.1 mM, are most effecient with 88% and 62% reactivation
iodoacetate
-
0.1 mM and 1 mM, 110.5% and 94.8% compared to a control without additives
iodoacetate
-
40% inhibition at a concentration of 5 mM, irreversible inhibition, no reactivation by addition of bivalent metal ions or SH-protecting reagents like cysteine and beta-mercaptomethanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no effect by addition of FAD, FMN, NADPH, NADP+, NADH, NAD+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 5.4
-
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly as substrate, 50 mM sodium acetate buffer
6 - 6.2
-
benzyloxycarbonyl-Gly-Leu as substrate, in presence of 0.5 M NaCl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2 - 6.5
-
pH 4.2: 28% of the maximal activity, pH 6.5: 43% of the maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
integral membrane protein, destined for the vacuolar lumen
-
sorting of integral membrane protein Cps1p into the luminal vesicles of multivesicular bodies
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GFP-Cps1p expressed in rsp5delta cells expressing wild-type or mutant HA-Rsp5p with WW domain mutations W257A, W359A, and W415A. GFP-Cps1p expressed in rsp5delta cells expressing HARsp5pWT, HA-rsp5pL733S or HA-rsp5G555D. GFP-Cps1p expressed in tul1delta cells, bsd2delta cells and sna3delta cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
CPS1 accumulates at an aberrant late endosomal compartment in mutants of the COPIB subcomplex. CPS1 is not delivered to the vacuolar lumen in COPIb mutants. Only mutations in COPIb subunits have an effect upon CPS1 sorting, whereas in COPIf mutants CPS1 localizes to the vacuolar lumen
additional information
-
GFP-Cps1p accumulates in a prevacuolar compartment as well as on the limiting membrane of the vacuole in rps5WW1-3 cells with WW domain mutations. In rsp5L733S cells, GFP-Cps1p is detectable in the lumen of the vacuole, some is also found on the limiting membrane of the vacuole. In bsd2delta cells, GFP-Cps1p accumulates in the limiting membrane of the vacuole. In tul1delta cells sorting is also impaired. No defect in GFP-Cps1p vacuolar sorting in sna3delta cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
sorting of Cps1p into the luminal vesicles of multivesicular bodies requires ubiquitination of their cytosolic domains by the ubiquitin ligases Rsp5p and/or Tul1p, whereas Sna3p, another integral membrane protein, does not require ubiquitination for entry into multivesicular bodies. Sna3p follows an ubiquitination-independent, but Rsp5p-mediated, sorting pathway to the vacuole
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 3.4.17.4)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
