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Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
Substrates: human anaphylatoxin C3A fragment 70-77
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Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
benzoyl-Ala-Arg + H2O
benzoyl-Ala + Arg
Substrates: -
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benzoyl-Ala-Lys + H2O
benzoyl-Ala + Lys
-
Substrates: -
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benzoyl-Asn-Arg + H2O
benzoyl-Asn + Arg
Substrates: -
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benzoyl-Gln-Arg + H2O
benzoyl-Gln + Arg
Substrates: -
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benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
benzoyl-Gly-argininic acid + H2O
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Substrates: -
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benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
Substrates: -
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benzoyl-Gly-L-Arg + H2O
benzoyl-Gly + L-Arg
Substrates: -
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benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
benzoyl-His-Arg + H2O
benzoyl-His + Arg
Substrates: -
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benzoyl-Ile-Arg + H2O
benzoyl-Ile + Arg
Substrates: -
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benzoyl-L-Asn-L-Arg + H2O
benzoyl-L-Asn + L-Arg
Substrates: -
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benzoyl-Leu-Arg + H2O
benzoyl-Leu + Arg
Substrates: -
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benzoyl-Met-Arg + H2O
benzoyl-Met + Arg
Substrates: -
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benzoyl-Phe-Arg + H2O
benzoyl-Phe + Arg
Substrates: -
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benzoyl-Ser-Arg + H2O
benzoyl-Ser + Arg
Substrates: -
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benzoyl-Thr-Arg + H2O
benzoyl-Thr + Arg
Substrates: -
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benzoyl-Trp-Arg + H2O
benzoyl-Trp + Arg
Substrates: -
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benzoyl-Tyr-Arg + H2O
benzoyl-Tyr + Arg
Substrates: -
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benzoyl-Val-Arg + H2O
benzoyl-Val + Arg
Substrates: -
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bradykinin(-Phe-Arg) + H2O
?
Substrates: -
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dansyl-Ala-Arg + H2O
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Substrates: substrate for determination of CPM activity
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Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
dynorphin A(1-13) + H2O
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu + Lys
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Substrates: i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
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EGF + H2O
des-Arg53-EGF + arginine
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Substrates: EGF, epidermal growth factor
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epidermal growth factor + H2O
dea-Arg53-epidermal growth factor + arginine
-
Substrates: -
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furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
Substrates: -
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furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
Substrates: -
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furylacryloyl-L-Ala-L-Arg + H2O
furylacryloyl-L-Ala + L-Arg
-
Substrates: -
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Gly-Gly-Arg + H2O
Gly-Gly + Arg
Substrates: -
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Gly-Leu-Ala-Arg + H2O
Gly-Leu-Ala + Arg
Substrates: human anaphylatoxin C3A fragment 74-77
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Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
Substrates: -
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His-Leu-Gly-Leu-Ala-Arg + H2O
His-Leu-Gly-Leu-Ala + Arg
Substrates: human anaphylatoxin C3A fragment 72-77
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Leu-Ala-Arg + H2O
Leu-Ala + Arg
Substrates: human anaphylatoxin C3A fragment 75-77
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Leu-Gly-Leu-Ala-Arg + H2O
Leu-Gly-Leu-Ala + Arg
Substrates: human anaphylatoxin C3A fragment 73-77
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Leu5-Arg6-enkephalin + H2O
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-
Substrates: -
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Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
Met5-Arg6-enkephalin + H2O
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-
Substrates: -
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Met5-Lys6-enkephalin + H2O
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-
Substrates: -
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N-(4-hydroxybenzoyl)-Gly-Arg + H2O
N-(4-hydroxybenzoyl)-Gly + L-arginine
Substrates: -
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Pro-Gly-Lys-Ala-Arg + H2O
Pro-Gly-Lys-Ala + Arg
Substrates: -
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SDF-1alpha + H2O
des-lys SDF-1alpha + lysine
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Substrates: stromal cell-derived factor
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Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ser-His-Leu-Gly-Leu-Ala + Arg
Substrates: human anaphylatoxin C3A fragment 71-77
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additional information
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Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
Substrates: bradykinin
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Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
Substrates: bradykinin
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Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
Substrates: bradykinin
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benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
Substrates: -
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benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
Substrates: -
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benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
Substrates: -
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benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
Substrates: -
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bradykinin + H2O
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Substrates: release of Arg9
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bradykinin + H2O
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-
Substrates: -
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Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
-
Substrates: -
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Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
Substrates: enzyme assay
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Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
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Substrates: substrate used in activity assay
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dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
-
Substrates: -
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dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
-
Substrates: -
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dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
Substrates: -
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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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Substrates: kallidin
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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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Substrates: kallidin
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additional information
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-
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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
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additional information
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Substrates: the enzyme might be involved in regulating the biological effects of complement anaphylatoxins at sites of tissue injury
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additional information
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Substrates: 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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Substrates: 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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Substrates: removing of the C-terminal Arg residue of the intact kinins and related peptides
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additional information
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Substrates: 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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Substrates: 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)
Products: -
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Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
Substrates: bradykinin
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EGF + H2O
des-Arg53-EGF + arginine
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Substrates: EGF, epidermal growth factor
Products: -
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epidermal growth factor + H2O
dea-Arg53-epidermal growth factor + arginine
-
Substrates: -
Products: -
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additional information
?
-
additional information
?
-
-
Substrates: the enzyme may be responsible for control of kinins and epidermal growth factor as well as of EGF-like peptides
Products: -
?
additional information
?
-
-
Substrates: the enzyme could inactivate or modulate the activity of peptide hormones either before or after their interaction with plasma membrane receptors
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the enzyme might be involved in regulating the biological effects of complement anaphylatoxins at sites of tissue injury
Products: -
?
additional information
?
-
Substrates: the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane
Products: -
?
additional information
?
-
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Substrates: the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
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additional information
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-
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Substrates: 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)
Products: -
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KCl
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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
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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
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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%
additional information
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the enzyme is a metallopeptidase
Co2+
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CoCl2 activates
Co2+
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CoCl2 activates more than 6-fold at pH 5.5, less than 2-fold at pH 7.5
Co2+
-
activates, best at acidic pH
Zn2+
-
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Zn2+
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the enzyme is a metallopeptidase, binding to His66
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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