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Enzyme Nomenclature
Information on EC 3.4.17.4 - Gly-Xaa carboxypeptidase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.17.4
-
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RECOMMENDED NAME
GeneOntology No.
Gly-Xaa carboxypeptidase
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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
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, C-terminus, amino acid
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-25-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
?
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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
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no effect by addition of FAD, FMN, NADPH, NADP+, NADH, NAD+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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
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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
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.17.4)
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