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Information on EC 3.4.17.12 - carboxypeptidase M
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3.4.17.12 carboxypeptidase MSpecify your search results
Word Map
- 3.4.17.12
- pain
- women
- lymphocyte
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contralateral
- children
-
postoperative
-
prophylactic
- myelinolysis
-
mastectomy
- pontine
- knee
- cyclophosphamide
-
unilateral
-
wave
-
rehabilitation
- hyponatremia
-
decision
-
summation
-
session
-
flexion
-
accelerometer
-
myoelectrical
-
chlorpheniramine
-
preoperative
-
arthroplasty
-
noxious
- phytohemagglutinin
-
3h-thymidine
- maleate
-
pressor
-
pain-free
-
decision-making
-
analgesia
-
psychophysical
-
actigraph
-
pokeweed
-
moderate-to-vigorous
-
3h-tdr
-
disomy
-
myotomy
-
cuff
-
physiotherapy
-
arthroscopic
-
gastroparesis
-
suprathreshold
- dysrhythmias
-
breast-conserving
- medicine
-
trapezius
-
manometry
-
resting-state
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
cpm, carboxypeptidase m, carboxypeptidase-m, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxypeptidase M
CPM
M14006 (Merops-ID)
-
-
-
-
additional information
-
the enzyme belongs to the CPN subgroup of mammalian carboxypeptidases
carboxypeptidase M
-
-
CPM
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of C-terminal arginine or lysine residues from polypeptides
a membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family)
-
-
-
cleavage of C-terminal arginine or lysine residues from polypeptides
catalytic mechanism, active site groove structure involving residues Y242, W241, K228, K269, E264, R127, H66, E69, and H173, substrate interactins
cleavage of C-terminal arginine or lysine residues from polypeptides
substrate binding via residue Tyr266
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
120038-28-0
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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
Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 70-77
-
-
?
dynorphin A(1-13) + H2O
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu + Lys
-
i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
-
?
epidermal growth factor + H2O
dea-Arg53-epidermal growth factor + arginine
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-
-
-
?
Gly-Leu-Ala-Arg + H2O
Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 74-77
-
-
?
His-Leu-Gly-Leu-Ala-Arg + H2O
His-Leu-Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 72-77
-
-
?
Leu-Ala-Arg + H2O
Leu-Ala + Arg
human anaphylatoxin C3A fragment 75-77
-
-
?
Leu-Gly-Leu-Ala-Arg + H2O
Leu-Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 73-77
-
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
N-(4-hydroxybenzoyl)-Gly-Arg + H2O
N-(4-hydroxybenzoyl)-Gly + L-arginine
-
-
-
?
SDF-1alpha + H2O
des-lys SDF-1alpha + lysine
-
stromal cell-derived factor
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-
?
Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ser-His-Leu-Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 71-77
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
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bradykinin
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
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bradykinin
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
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bradykinin
-
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
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kallidin
-
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
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kallidin
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-
?
additional information
?
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the enzyme may be responsible for control of kinins and epidermal growth factor as well as of EGF-like peptides
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-
?
additional information
?
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carboxypeptidase M does not hydrolyze the peptidyl dipeptidase substrate furylacryloyl-Phe-Gly-Gly or the carboxypeptidase A substrates benzoyl-Gly-phenyllactic acid and furylacryloyl-Phe-Phe
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-
?
additional information
?
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the enzyme could inactivate or modulate the activity of peptide hormones either before or after their interaction with plasma membrane receptors
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-
?
additional information
?
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the enzyme controls the activity of kinins in the kidney, is involved in inflammation, and participates in the metabolism of growth factors that contain C-terminal Arg or Lys residues, e.g. the epidermal growth factor, the nerve growth factor, the hypatocyte growth factor, the macrophage-stimulating protein, or erythropoietin
-
-
?
additional information
?
-
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the enzyme might be involved in regulating the biological effects of complement anaphylatoxins at sites of tissue injury
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-
?
additional information
?
-
the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane
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-
?
additional information
?
-
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the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane
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-
?
additional information
?
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removing of the C-terminal Arg residue of the intact kinins and related peptides
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-
?
additional information
?
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using small substrates of the form benzoyl-Xaa-Arg CPM has the highest catalytic efficiency for substrates with the nonpolar aliphatic residues Ala and Met and aromatic amino acids (Phe, Tyr, Trp) in the penultimate place and the lowest with branched side chains (Ile)
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-
?
additional information
?
-
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using small substrates of the form benzoyl-Xaa-Arg CPM has the highest catalytic efficiency for substrates with the nonpolar aliphatic residues Ala and Met and aromatic amino acids (Phe, Tyr, Trp) in the penultimate place and the lowest with branched side chains (Ile)
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-
?
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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
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
bradykinin
-
-
?
epidermal growth factor + H2O
dea-Arg53-epidermal growth factor + arginine
-
-
-
-
?
additional information
?
-
-
the enzyme may be responsible for control of kinins and epidermal growth factor as well as of EGF-like peptides
-
-
?
additional information
?
-
-
the enzyme could inactivate or modulate the activity of peptide hormones either before or after their interaction with plasma membrane receptors
-
-
?
additional information
?
-
-
the enzyme controls the activity of kinins in the kidney, is involved in inflammation, and participates in the metabolism of growth factors that contain C-terminal Arg or Lys residues, e.g. the epidermal growth factor, the nerve growth factor, the hypatocyte growth factor, the macrophage-stimulating protein, or erythropoietin
-
-
?
additional information
?
-
-
the enzyme might be involved in regulating the biological effects of complement anaphylatoxins at sites of tissue injury
-
-
?
additional information
?
-
the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane
-
-
?
additional information
?
-
-
the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane
-
-
?
additional information
?
-
using small substrates of the form benzoyl-Xaa-Arg CPM has the highest catalytic efficiency for substrates with the nonpolar aliphatic residues Ala and Met and aromatic amino acids (Phe, Tyr, Trp) in the penultimate place and the lowest with branched side chains (Ile)
-
-
?
additional information
?
-
-
using small substrates of the form benzoyl-Xaa-Arg CPM has the highest catalytic efficiency for substrates with the nonpolar aliphatic residues Ala and Met and aromatic amino acids (Phe, Tyr, Trp) in the penultimate place and the lowest with branched side chains (Ile)
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
KCl
-
addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wilde-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
KNO3
-
addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wilde-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
Na2SO4
-
addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wilde-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
NaCl
-
addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wilde-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
NaNO3
-
addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wilde-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
Zn2+
Zn2+
the catalytic center is located in the catalytic domain in a cavity with a funnel-like access that contains the catalytic Zn2+ ion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression level of the gene carboxypeptidase M decreased after a Salmonella infection
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2-mercaptomethyl-3-guanidinoethyl thiopropanoic acid
strong CPM inhibitor
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
specific carboxypeptidase M inhibitor
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
specific carboxypeptidase M inhibitor
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
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inhibits best at acidic pH
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IFN-gamma
-
CPM activity can be upregulated approximately two-fold in HLMVECs by IL-1beta plus IFN-gamma treatment
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IL-1beta
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CPM activity can be upregulated approximately two-fold in HLMVECs by IL-1beta plus IFN-gamma treatment, IL-1beta alone can upregulate CPM expression
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lipopolysaccharide
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following stimulation with bacterial lipopolysaccharide a marginal upregulation of the expression of carboxypeptidase M is observed
additional information
-
there is a spatial proximity and interaction between angiotensin-converting enzyme and endogenous carboxypeptidase M in MDCK cells, as well as a weak but detectable release of glycosylphosphatidylinositol-anchored carboxypeptidase M evoked by co-localized between angiotensin-converting enzyme
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additional information
-
there is a spatial proximity and interaction between angiotensin-converting enzyme and endogenous carboxypeptidase M in CHO cells, as well as a weak but detectable release of glycosylphosphatidylinositol-anchored carboxypeptidase M evoked by co-localized between angiotensin-converting enzyme
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additional information
-
prolactin/17beta-estradiol does not increase carboxypeptidase M expression
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.059
Dansyl-Ala-Arg
-
wild-type enzyme lacking the C-terminal hydrophobic membrane anchor signal
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE