Information on EC 3.4.17.4 - Gly-Xaa carboxypeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.17.4
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RECOMMENDED NAME
GeneOntology No.
Gly-Xaa carboxypeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
from yeast. In peptidase family M20, glutamate carboxypeptidase family
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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exopeptidase, C-terminus, amino acid
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-25-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly + H2O
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe
show the reaction diagram
benzoyl-Gly-Gly + H2O
?
show the reaction diagram
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7.2% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
benzoyl-Gly-Lys + H2O
?
show the reaction diagram
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2% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
benzyloxycarbonyl-Ala-Arg(NO2) + H2O
benzyloxycarbonyl-Ala + nitroarginine
show the reaction diagram
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21% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
show the reaction diagram
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10% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
Benzyloxycarbonyl-Glu-Tyr + H2O
Benzyloxycarbonyl-Glu + Tyr
show the reaction diagram
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1.1% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
benzyloxycarbonyl-Gly-Glu + H2O
benzyloxycarbonyl-Gly + Glu
show the reaction diagram
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31% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
benzyloxycarbonyl-Gly-Gly + H2O
benzyloxycarbonyl-Gly + Gly
show the reaction diagram
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13% of the activity compared to benzyloxycarbonyl-Gly-Leu
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?
Benzyloxycarbonyl-Gly-Leu + H2O
Benzyloxycarbonyl-Gly + Leu
show the reaction diagram
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best substrate
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-
?
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
show the reaction diagram
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31% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
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1.5% of the activity compared to benzyloxycarbonyl-Gly-Leu
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?
benzyloxycarbonyl-Phe-Met + H2O
benzyloxycarbonyl-Phe + Met
show the reaction diagram
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1.5% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
benzyloxycarbonyl-Phe-Phe + H2O
benzyloxycarbonyl-Phe + Phe
show the reaction diagram
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1.5% of the activity compared to benzyloxycarbonyl-Gly-Leu
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-
?
dibenzyloxycarbonyl-Lys-Leu + H2O
dibenzyloxycarbonyl-Lys + Leu
show the reaction diagram
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5.2% of the activity compared to benzyloxycarbonyl-Gly-Leu
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?
Gly-Leu-Gly + H2O
?
show the reaction diagram
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3% of the activity compared to benzyloxycarbonyl-Gly-Leu
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?
Gly-Leu-Tyr + H2O
?
show the reaction diagram
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12% of the activity compared to benzyloxycarbonyl-Gly-Leu
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?
additional information
?
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
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0.1 mM and 1 mM, 108.9% and 105.5% compared to a control without additives
Cd2+
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can reverse the inhibition by chelating agents
Co2+
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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
MgCl2
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0.1 mM and 1 mM, 109.8% and 103.4% compared to a control without additives
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
CuSO4
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complete inhibition at 1 mM, 39% inhibition at 0.1 mM
diisopropylphosphorofluoridate
iodoacetamide
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90% inhibition at a concentration of 5 mM
iodoacetate
p-chloromercuribenzoate
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irreversible inhibition, no reactivation by addition of bivalent metal ions or SH-protecting reagents like cysteine and beta-mercaptomethanol
p-Chloromercuriphenylsulfonic acid
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0.1 mM and 1 mM, complete inhibition
PMSF
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0.1 mM and 1 mM, 78.1% and 21.4% compared to a control without additives
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no effect by addition of FAD, FMN, NADPH, NADP+, NADH, NAD+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0211
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000000113
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six-week-old animal
0.000000115
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six-week-old animal
0.000000116
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six-week-old animal
0.000001917
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six-week-old animal
0.00000415
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six-week-old animal
0.00000845
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six-week-old animal
230
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 5.4
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4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly as substrate, 50 mM sodium acetate buffer
6 - 6.2
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benzyloxycarbonyl-Gly-Leu as substrate, in presence of 0.5 M NaCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2 - 6.5
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pH 4.2: 28% of the maximal activity, pH 6.5: 43% of the maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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plasmid pGFP-CPS1, which expresses GFP-CPS1
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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