Information on EC 3.4.17.16 - membrane Pro-Xaa carboxypeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.17.16
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RECOMMENDED NAME
GeneOntology No.
membrane Pro-Xaa carboxypeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
9075-64-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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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
Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + Ala
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro- + Ala
show the reaction diagram
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-
-
-
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro + Ala
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Leu-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Leu-Gly-Pro + Ala
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Pro-Ala + H2O
Benzyloxycarbonyl-Pro + Ala
show the reaction diagram
Benzyloxycarbonyl-Pro-Gly + H2O
Benzyloxycarbonyl-Pro + Gly
show the reaction diagram
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-
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Benzyloxycarbonyl-Pro-Met + H2O
Benzyloxycarbonyl-Pro + Met
show the reaction diagram
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-
-
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Benzyloxycarbonyl-Pro-Phe + H2O
Benzyloxycarbonyl-Pro + Phe
show the reaction diagram
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-
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hirudin variant 3 + H2O
?
show the reaction diagram
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HPLC-ESI-ITMS is used as atool to confirm the C-terminal sequence of HV3, the degradation of the C-terminal of HV3 is studied using carboxypeptidase P und Y
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?
Myoglobin + H2O
?
show the reaction diagram
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?
prekallikrein + H2O
?
show the reaction diagram
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the potential PRCP cleavage site on prekallikrein is identified based on molecular modelling
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?
Val-Ala-Ala-Phe + H2O
Val-Ala-Ala + Phe
show the reaction diagram
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additional information
?
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peptides free of proline are also cleaved, but normally at a rather low rate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn
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each of the two subunits contains one Zn atom, ZnSO4, 0.5 mM, limited activation in absence of MnCl2, strong inhibition above 0.5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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EDTA
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Zn2+
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0.5 mM activates, inhibition above
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dexamethasone
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up-regulation the gene expression subsequent to 48 h treatment of SH-SY5Y cells with 30 nM dexamethasone plus 1 nM [D-Ala2, N-Me-Phe4, Gly5-ol]-enkephalin acetate
[D-Ala2, N-Me-Phe4, Gly5-ol]-enkephalin acetate
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up-regulation the gene expression subsequent to 48 h treatment of SH-SY5Y cells with 30 nM dexamethasone plus 1 nM [D-Ala2, N-Me-Phe4, Gly5-ol]-enkephalin acetate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
Benzyloxycarbonyl-Pro-Met
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0.1 - 0.13
Myoglobin
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.5
Benzyloxycarbonyl-Pro-Met
Sus scrofa
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0.3 - 1.1
Myoglobin
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
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enzyme reaction on the QCM plate; hydrolysis of myoglobin in bulk solution
7.8
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in presence of 1 mM MnCl2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 6
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enzyme reaction on the QCM plate
2.5 - 5
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hydrolysis of myoglobin in bulk solution
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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enzyme reaction on the QCM plate; hydrolysis of myoglobin in bulk solution
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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neuroblastoma cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135000
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2 * 135000, pig, SDS-PAGE
240000
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pig, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 135000, pig, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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0.332 mg carbohydrate per mg of protein including 23% mannose, 29% galactose, 30% N-acetylglucosamine, 7% glucose and 11% uncharacterized sugar
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, unstable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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results from the study could provide new therapeutic opportunity for the treatment of infection