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Information on EC 3.4.17.10 - carboxypeptidase E
for references in articles please use BRENDA:EC3.4.17.10
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.17 Metallocarboxypeptidases
3.4.17.10 carboxypeptidase E
IUBMB Comments
A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family).
The enzyme appears in viruses and cellular organisms
- 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
showSynonyms
cpe, carboxypeptidase e, carboxypeptidase h, metallocarboxypeptidase, enkephalin convertase, membrane-bound carboxypeptidase, egl-21, carboxypeptidase e/h, prohormone processing carboxypeptidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase E
carboxypeptidase, enkephalin precursor
-
-
-
-
cobalt stimulated chromaffin granule carboxypeptidase
-
-
-
-
CPE
CPE-NFalpha1
CPH
-
-
-
-
enkephalin convertase
enkephalin precursor carboxypeptidase
-
-
-
-
enkephalin-precursor endopeptidase
-
-
-
-
insulin granule-associated carboxypeptidase
-
-
-
-
membrane-bound carboxypeptidase
-
-
-
-
neurotrophic factor-alpha1
peptidyl-L-lysine(-L-arginine) hydrolase
-
-
-
-
Prohormone processing carboxypeptidase
-
-
-
-
additional information
carboxypeptidase E
-
-
-
-
carboxypeptidase E
-
-
CPE
-
-
-
-
CPE
-
-
enkephalin convertase
-
-
-
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dansyl-Phe-Leu-Ala-Arg + H2O
dansyl-Phe-Leu-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
dansyl-Phe-Leu-Gly-Arg + H2O
dansyl-Phe-Leu-Gly + Arg
-
Substrates: -
Products: -
Products: -
?
iodo-acetyl-Tyr-Ala-Arg + H2O
iodo-acetyl-Tyr-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
[Leu5]enkephalin-Arg6-Arg7 + H2O
[Leu5]enkephalin + Arg
-
Substrates: -
Products: -
Products: -
?
(Met)enkephalin-Arg + H2O
Tyr-Gly-Gly-Phe-Met + Arg
-
Substrates: -
Products: -
Products: -
?
(Met)enkephalin-Arg + H2O
Tyr-Gly-Gly-Phe-Met + Arg
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Substrates: -
Products: -
Products: -
?
(Met)enkephalin-Lys + H2O
Tyr-Gly-Gly-Phe-Met + Lys
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Substrates: -
Products: -
Products: -
?
(Met)enkephalin-Lys + H2O
Tyr-Gly-Gly-Phe-Met + Lys
-
Substrates: -
Products: -
Products: -
?
acetyl-Tyr-Ala-Arg + H2O
acetyl-Tyr-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
benzoyl-Phe-Ala-Arg + H2O
benzoyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
benzoyl-Phe-Ala-Arg + H2O
benzoyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
benzoyl-Phe-Ala-Arg + H2O
benzoyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
Dansyl-Phe-Ala-Arg + H2O
Dansyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
Dansyl-Phe-Ala-Arg + H2O
Dansyl-Phe-Ala + Arg
-
Substrates: -
Products: -
Products: -
?
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
Substrates: processing
Products: -
Products: -
?
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-islet amyloid polypeptide propeptide
-
Substrates: processing in pancreatic beta-cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for C-terminal basic amino acids in decreasing order: Arg, Lys,His, does not cleave other amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
Products: -
Products: -
?
additional information
?
-
-
Substrates: conversion of peptide hormone precursor into their smaller active forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: FMRFamide-like peptide (FLP) precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: neuropeptide-like protein (NLP) precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: conversion of peptide hormone precursor into their smaller active forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the CPE reaction trims off C-terminal basic residues of peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of C-terminal arginine or lysine residues from polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: CPE interacts with heparin which is shown by surface plasmon resonance (SPR) and in silico interaction analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the removal of C-terminal amino acids from proteins and peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
Products: -
Products: -
?
additional information
?
-
-
Substrates: carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds to secretogranin III
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of neuropeptides and peptide hormones
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of C-terminal arginine or lysine residues from polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for C-terminal basic amino acids in decreasing order: Arg, Lys,His, does not cleave other amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
Products: -
Products: -
?
additional information
?
-
-
Substrates: conversion of peptide hormone precursor into their smaller active forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of insulin in pancreatic beta-cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of C-terminal arginine or lysine residues from polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: releases C-terminal arginine or lysine residues from the hexapeptide precursor of [Met]enkephalin and [Leu]enkephalin, forming the pentapeptide enkephalin
Products: -
Products: -
?
additional information
?
-
-
Substrates: C-terminal histidine is removed at a very slow rate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
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
-
Substrates: processing in pancreatic beta-cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: conversion of peptide hormone precursor into their smaller active forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: FMRFamide-like peptide (FLP) precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: neuropeptide-like protein (NLP) precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: conversion of peptide hormone precursor into their smaller active forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of C-terminal arginine or lysine residues from polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: CPE interacts with heparin which is shown by surface plasmon resonance (SPR) and in silico interaction analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the removal of C-terminal amino acids from proteins and peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
Products: -
Products: -
?
additional information
?
-
-
Substrates: carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of neuropeptides and peptide hormones
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of C-terminal arginine or lysine residues from polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina
Products: -
Products: -
?
additional information
?
-
-
Substrates: conversion of peptide hormone precursor into their smaller active forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of insulin in pancreatic beta-cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly specific for C-terminal basic amino acids Arg in decreasing order: Arg, Lys, His, does not cleave other amino acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: altered biosynthesis of the neuropeptide processing enzyme after brain ischemia: molecular mechanism and implication
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme contributes to the sorting of proteins into the secretory pathway, and is involved in the biosynthesis of several peptide hormones and neurotransmitters
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of C-terminal arginine or lysine residues from polypeptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: C-terminal histidine is removed at a very slow rate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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+
NiCl2
Zn2+
additional information