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Information on EC 3.4.17.10 - carboxypeptidase E
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3.4.17.10 carboxypeptidase ESpecify your search results
Word Map
- 3.4.17.10
-
cytopathic
-
carbapenemase-producing
- enterobacteriaceae
- clostridium
- perfringens
- enterotoxin
- viruses
- carbapenemase
- pneumonia
-
electrode
- klebsiella
- neuropeptides
-
cloud
-
outbreak
-
preconcentration
-
carriage
-
swab
- enterobacterales
-
cytopathogenic
-
carba
- meropenem
-
voltammetric
-
polyelectrolyte
-
carbapenem-resistant
-
cardiogenic
-
blaoxa-48
- colistin
-
oxa-48-like
-
alpha-amidating
-
esbls
- enteroviruses
- imipenem
- vim
- ertapenem
- proinsulin
-
antibiotic-associated
- claudin-4
-
blakpc
-
tcid50
-
blandm
-
extended-spectrum
-
kpc-producing
- medicine
-
spiritual
- diagnostics
- blaimp
-
esbl-producing
-
parapneumonic
-
hodge
-
eucast
- biotechnology
- drug development
-
macconkey
-
stewardship
The enzyme appears in viruses and cellular organisms
Synonyms
cpe, carboxypeptidase e, carboxypeptidase h, metallocarboxypeptidase, enkephalin convertase, membrane-bound carboxypeptidase, egl-21, carboxypeptidase e/h, prohormone processing carboxypeptidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase E
carboxypeptidase, enkephalin precursor
-
-
-
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cobalt stimulated chromaffin granule carboxypeptidase
-
-
-
-
CPE
CPE-NFalpha1
CPH
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-
-
-
enkephalin convertase
enkephalin precursor carboxypeptidase
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-
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-
enkephalin-precursor endopeptidase
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-
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insulin granule-associated carboxypeptidase
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-
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membrane-bound carboxypeptidase
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-
-
-
neurotrophic factor-alpha1
peptidyl-L-lysine(-L-arginine) hydrolase
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-
-
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Prohormone processing carboxypeptidase
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-
-
-
additional information
carboxypeptidase E
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-
-
-
carboxypeptidase E
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-
CPE
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-
-
-
CPE
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-
enkephalin convertase
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-
-
-
additional information
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the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
additional information
-
the enzyme belongs to the family of metallocarboxypeptidases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of C-terminal arginine or lysine residues from polypeptides
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
exopeptidase, C-terminus, amino acid
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CAS REGISTRY NUMBER
COMMENTARY
81876-95-1
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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
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
processing
-
-
?
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
processing in pancreatic beta-cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids in decreasing order: Arg, Lys,His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
the enzyme is a sorting receptor for the regulated secretory pathway. The sorting receptor function of the enzyme necessitates its interaction with glycosphingolipid-cholesterol rafts at the trans-Golgi network, thereby anchoring it in position to bind to its prohormone cargo
-
?
additional information
?
-
-
the enzyme is a sorting receptor that directs the prohormone pro-opiomelanocortin to the regulated secretory pathway and is also a prohormone processing enzyme in neuro/endocrine cells
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
FMRFamide-like peptide (FLP) precursors
-
-
?
additional information
?
-
-
neuropeptide-like protein (NLP) precursors
-
-
?
additional information
?
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-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
the CPE reaction trims off C-terminal basic residues of peptides
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
carboxypeptidase E, a prohormone processing exopeptidase and sorting receptor for the regulated secretory pathway, interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function. Mammalian cell lines coexpressing carboxypeptidase E and dopamine transporter exhibit increased dopamine transporter-mediated dopamine uptake activity compared to cells expressing dopamine transporter alone. Moreover, coexpression of an interfering dopamine transporter-carboxyl terminus minigene inhibit the effects of carboxypeptidase E on dopamine transporter. Functional changes caused by carboxypeptidase E could be attributed to enhanced dopamine transporter expression and subsequent increase in dopamine transporter cell surface localization, due to decreased dopamine transporter degradation. In addition, carboxypeptidase E association could reduce the phosphorylation state of dopamine transporter on serine residues, potentially leading to reduced internalization, thus stabilizing plasmalemmal dopamine transporter localization
-
-
?
additional information
?
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-
CPE interacts with heparin which is shown by surface plasmon resonance (SPR) and in silico interaction analysis
-
-
?
additional information
?
-
-
catalyzes the removal of C-terminal amino acids from proteins and peptides
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules, both proteins form the separate functional sorting complex by anchoring in the cholesterol-rich membranes of the secretory granules, overview, secretogranin III can funtionally compensate for CPEin enzyme-defective mutant mice
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
biosynthesis of neuropeptides and peptide hormones
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids in decreasing order: Arg, Lys,His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
biosynthesis of insulin in pancreatic beta-cells
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
the enzyme removes C-terminal basic residues, Arg, Lys, and to a minor extent also His, from a variety of substrates, but shows no activity against nonbasic residues, the enzyme prefers Met at the P1 position but tolerates all amino acids, showing low activity in cleaving Pro-Arg bonds, it has a preference for tri- and tetrapeptides compared to dipeptides
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
-
-
?
additional information
?
-
-
C-terminal histidine is removed at a very slow rate
-
-
?
additional information
?
-
-
carboxypeptidase E interacts with the dopamine transporter carboxyl terminus and affects dopamine transporter function, carboxypeptidase E plays a role in the regulation of dopamine transporter trafficking and dopamine transporter-mediated dopamine uptake, which may provide a novel target in the treatment of dopamine-governed diseases such as drug addiction and obesity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
processing in pancreatic beta-cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information
?
-
-
the enzyme is a sorting receptor for the regulated secretory pathway. The sorting receptor function of the enzyme necessitates its interaction with glycosphingolipid-cholesterol rafts at the trans-Golgi network, thereby anchoring it in position to bind to its prohormone cargo
-
?
additional information
?
-
-
the enzyme is a sorting receptor that directs the prohormone pro-opiomelanocortin to the regulated secretory pathway and is also a prohormone processing enzyme in neuro/endocrine cells
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
FMRFamide-like peptide (FLP) precursors
-
-
?
additional information
?
-
-
neuropeptide-like protein (NLP) precursors
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
CPE interacts with heparin which is shown by surface plasmon resonance (SPR) and in silico interaction analysis
-
-
?
additional information
?
-
-
catalyzes the removal of C-terminal amino acids from proteins and peptides
-
-
?
additional information
?
-
-
altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules, both proteins form the separate functional sorting complex by anchoring in the cholesterol-rich membranes of the secretory granules, overview, secretogranin III can funtionally compensate for CPEin enzyme-defective mutant mice
-
-
?
additional information
?
-
-
the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
-
-
?
additional information
?
-
-
biosynthesis of neuropeptides and peptide hormones
-
-
?
additional information
?
-
-
release of C-terminal arginine or lysine residues from polypeptides
-
-
?
additional information
?
-
-
carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
-
-
?
additional information
?
-
-
conversion of peptide hormone precursor into their smaller active forms
-
-
?
additional information
?
-
-
biosynthesis of insulin in pancreatic beta-cells
-
-
?
additional information
?
-
-
highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin, associated with the biosynthesis of many peptide neurotransmitters and hormones
-
-
?
additional information