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Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 70-77
-
-
?
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
-
-
-
?
benzoyl-Ala-Lys + H2O
benzoyl-Ala + Lys
-
-
-
?
benzoyl-Asn-Arg + H2O
benzoyl-Asn + Arg
-
-
-
?
benzoyl-Gln-Arg + H2O
benzoyl-Gln + Arg
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
benzoyl-Gly-argininic acid + H2O
?
-
-
-
?
benzoyl-Gly-argininic acid + H2O
benzoyl-Gly + argininic acid
-
-
-
?
benzoyl-Gly-L-Arg + H2O
benzoyl-Gly + L-Arg
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
benzoyl-His-Arg + H2O
benzoyl-His + Arg
-
-
-
?
benzoyl-Ile-Arg + H2O
benzoyl-Ile + Arg
-
-
-
?
benzoyl-L-Asn-L-Arg + H2O
benzoyl-L-Asn + L-Arg
-
-
-
?
benzoyl-Leu-Arg + H2O
benzoyl-Leu + Arg
-
-
-
?
benzoyl-Met-Arg + H2O
benzoyl-Met + Arg
-
-
-
?
benzoyl-Phe-Arg + H2O
benzoyl-Phe + Arg
-
-
-
?
benzoyl-Ser-Arg + H2O
benzoyl-Ser + Arg
-
-
-
?
benzoyl-Thr-Arg + H2O
benzoyl-Thr + Arg
-
-
-
?
benzoyl-Trp-Arg + H2O
benzoyl-Trp + Arg
-
-
-
?
benzoyl-Tyr-Arg + H2O
benzoyl-Tyr + Arg
-
-
-
?
benzoyl-Val-Arg + H2O
benzoyl-Val + Arg
-
-
-
?
bradykinin(-Phe-Arg) + H2O
?
-
-
-
?
dansyl-Ala-Arg + H2O
?
-
substrate for determination of CPM activity
-
-
?
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
-
i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
-
?
EGF + H2O
des-Arg53-EGF + arginine
-
EGF, epidermal growth factor
-
-
?
epidermal growth factor + H2O
dea-Arg53-epidermal growth factor + arginine
-
-
-
-
?
furylacryloyl-Ala-Arg + H2O
furylacryloyl-Ala + Arg
-
-
-
?
furylacryloyl-Ala-Lys + H2O
furylacryloyl-Ala + Lys
-
-
-
?
furylacryloyl-L-Ala-L-Arg + H2O
furylacryloyl-L-Ala + L-Arg
-
-
-
-
?
Gly-Gly-Arg + H2O
Gly-Gly + Arg
-
-
-
?
Gly-Leu-Ala-Arg + H2O
Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 74-77
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
?
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
-
-
?
Leu5-Arg6-enkephalin + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
Met5-Lys6-enkephalin + H2O
?
-
-
-
-
?
N-(4-hydroxybenzoyl)-Gly-Arg + H2O
N-(4-hydroxybenzoyl)-Gly + L-arginine
-
-
-
?
Pro-Gly-Lys-Ala-Arg + H2O
Pro-Gly-Lys-Ala + Arg
-
-
-
?
SDF-1alpha + H2O
des-lys SDF-1alpha + lysine
-
stromal cell-derived factor
-
-
?
Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ser-His-Leu-Gly-Leu-Ala + Arg
human anaphylatoxin C3A fragment 71-77
-
-
?
additional information
?
-
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
bradykinin
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
bradykinin
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
bradykinin
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
-
?
benzoyl-Gly-Arg + H2O
benzoyl-Gly + Arg
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
-
-
-
?
benzoyl-Gly-Lys + H2O
benzoyl-Gly + Lys
-
-
-
?
bradykinin + H2O
?
-
release of Arg9
-
-
?
bradykinin + H2O
?
-
-
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
-
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
-
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
-
-
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
enzyme assay
-
-
?
Dansyl-Ala-Arg + H2O
Dansyl-Ala + Arg
-
substrate used in activity assay
-
-
?
dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
-
-
-
-
?
dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
-
-
-
-
?
dansyl-L-Ala-L-Arg + H2O
dansyl-L-Ala + L-Arg
-
-
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
kallidin
-
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + arginine
-
kallidin
-
-
?
additional information
?
-
-
the enzyme may be responsible for control of kinins and epidermal growth factor as well as of EGF-like peptides
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
removing of the C-terminal Arg residue of the intact kinins and related peptides
-
-
?
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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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%
additional information
-
the enzyme is a metallopeptidase
Co2+
-
CoCl2 activates
Co2+
-
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+
-
-
Zn2+
-
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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Deddish, P.A.; Skidgel, R.A.; Erds, E.G.
Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)
Biochem. J.
261
289-291
1989
Homo sapiens
brenda
Skidgel, R.A.; Davis, R.M.; Tan, F.
Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones
J. Biol. Chem.
264
2236-2241
1989
Homo sapiens
brenda
Tan, F.; Deddish, P.A.; Skidgel, R.A.
Human carboxypeptidase M
Methods Enzymol.
248
663-675
1995
Homo sapiens
brenda
Deddish, P.A.; Skidgel, R.A.; Kriho, V.B.; Li, X.Y.; Becker, R.P.; Erds, E.G.
Carboxypeptidase M in Madin-Darby canine kidney cells. Evidence that carboxypeptidase M has a phosphatidylinositol glycan anchor
J. Biol. Chem.
265
15083-15089
1990
Canis lupus familiaris
brenda
Tan, F.; Balsitis, S.; Black, J.K.; Blochl, A.; Mao, J.F.; Becker, R.P.; Schacht, D.; Skidgel, R.A.
Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring
Biochem. J.
370
567-578
2003
Homo sapiens
brenda
Craveiro, R.B.; Ramalho, J.D.; Chagas, J.R.; Wang, P.H.; Casarini, D.; Pesquero, J.L.; Araujo, R.C.; Pesquero, J.B.
High expression of human carboxypeptidase M in Pichia pastoris: purification and partial characterization
Braz. J. Med. Biol. Res.
39
211-217
2006
Homo sapiens
brenda
Skidgel, R.A.
Carboxypeptidase M
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) Academic Press
2
851-854
2004
Canis lupus familiaris, Homo sapiens
-
brenda
Reverter, D.; Maskos, K.; Tan, F.; Skidgel, R.A.; Bode, W.
Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity
J. Mol. Biol.
338
257-269
2004
Homo sapiens (P14384), Homo sapiens
brenda
Matthews, K.W.; Mueller-Ortiz, S.L.; Wetsel, R.A.
Carboxypeptidase N: a pleiotropic regulator of inflammation
Mol. Immunol.
40
785-793
2004
Homo sapiens
brenda
Ahmad, M.; Zeitlin, I.J.; Parratt, J.R.; Pitt, A.R.
Degradation of bradykinin, a cardioprotective substance, during a single passage through isolated rat-heart
Arch. Pharm. Res.
29
241-248
2006
Rattus norvegicus
brenda
Deiteren, K.; Surpateanu, G.; Gilany, K.; Willemse, J.L.; Hendriks, D.F.; Augustyns, K.; Laroche, Y.; Scharpe, S.; Lambeir, A.M.
The role of the S1 binding site of carboxypeptidase M in substrate specificity and turn-over
Biochim. Biophys. Acta
1774
267-277
2007
Homo sapiens (P14384)
brenda
Skidgel, R.A.; Stanisavljevic, S.; Erdoes, E.G.
Kinin- and angiotensin-converting enzyme (ACE) inhibitor-mediated nitric oxide production in endothelial cells
Biol. Chem.
387
159-165
2006
Bos taurus, Homo sapiens
brenda
Schremmer-Danninger, E.; Naegler, D.K.; Miska, K.; Flaig, M.J.; Faussner, A.; Fink, E.; Raggi, M.C.; Jochum, M.; Rehbock, J.
Kinin receptors in stimulated and characterized decidua tissue-derived cells
Int. Immunopharmacol.
7
103-112
2007
Homo sapiens
brenda
Zhang, X.; Tan, F.; Zhang, Y.; Skidgel, R.A.
Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient B1 signaling from B2 agonists
J. Biol. Chem.
283
7994-8004
2008
Homo sapiens
brenda
Tsakiris, I.; Soos, G.; Nemes, Z.; Kiss, S.S.; Andras, C.; Szanto, J.; Dezso, B.
The presence of carboxypeptidase-M in tumour cells signifies epidermal growth factor receptor expression in lung adenocarcinomas: The coexistence predicts a poor prognosis regardless of EGFR levels
J. Cancer Res. Clin. Oncol.
134
439-451
2008
Homo sapiens
brenda
Fujiwara, H.
Membrane-bound peptidases regulate human extravillous trophoblast invasion
Placenta
28 Suppl A
S70-S75
2007
Homo sapiens
brenda
Fujiwara, N.; Ikeda, M.; Hirabayashi, S.; Mori, H.; Shirasawa, M.; Kansaku, A.; Sunamori, M.; Hata, Y.
Monoclonal antibody 7F9 recognizes rat protein homologous to human carboxypeptidase-M in developing and adult rat lung
Respirology
12
54-62
2007
Rattus norvegicus
brenda
Marquez-Curtis, L.; Jalili, A.; Deiteren, K.; Shirvaikar, N.; Lambeir, A.M.; Janowska-Wieczorek, A.
Carboxypeptidase M expressed by human bone marrow cells cleaves the C-terminal lysine of SDF-1{alpha}: Another player in hematopoietic stem/progenitor cell mobilization?
Stem Cells
26
1211-1220
2008
Homo sapiens
brenda
van Hemert, S.; Hoekman, A.J.; Smits, M.A.; Rebel, J.M.
Immunological and gene expression responses to a Salmonella infection in the chicken intestine
Vet. Res.
38
51-63
2006
Gallus gallus
brenda
Sun, X.; Wiesner, B.; Lorenz, D.; Papsdorf, G.; Pankow, K.; Wang, P.; Dietrich, N.; Siems, W.E.; Maul, B.
Interaction of angiotensin-converting enzyme (ACE) with membrane-bound carboxypeptidase M (CPM) - a new function of ACE
Biol. Chem.
389
1477-1485
2008
Canis lupus familiaris, Cricetulus griseus
brenda
Guimaraes, A.O.; Motta, F.L.; Alves, V.S.; Castilho, B.A.; Pesquero, J.B.
Multiple RNAs from the mouse carboxypeptidase M locus: functional RNAs or transcription noise?
BMC Mol. Biol.
10
7-7
2009
Mus musculus (Q80V42), Mus musculus
brenda
Deiteren, K.; Hendriks, D.; Scharpe, S.; Lambeir, A.M.
Carboxypeptidase M: Multiple alliances and unknown partners
Clin. Chim. Acta
399
24-39
2009
Homo sapiens (P14384), Homo sapiens
brenda
Abdelmagid, S.A.; Too, C.K.
Prolactin and estrogen up-regulate carboxypeptidase-D to promote nitric oxide production and survival of MCF-7 breast cancer cells
Endocrinology
149
4821-4828
2008
Homo sapiens
brenda
De Beuf, A.; Hou, X.H.; DHaese, P.C.; Verhulst, A.
Epoetin delta reduces oxidative stress in primary human renal tubular cells
J. Biomed. Biotechnol.
2010
395785
2010
Homo sapiens
brenda
Erickson-Johnson, M.R.; Seys, A.R.; Roth, C.W.; King, A.A.; Hulshizer, R.L.; Wang, X.; Asmann, Y.W.; Lloyd, R.V.; Jacob, E.K.; Oliveira, A.M.
Carboxypeptidase M: a biomarker for the discrimination of well-differentiated liposarcoma from lipoma
Mod. Pathol.
22
1541-1547
2009
Homo sapiens
brenda
Zhang, X.; Tan, F.; Skidgel, R.A.
Carboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor
J. Biol. Chem.
288
33226-33240
2013
Homo sapiens (P14384), Homo sapiens
brenda
Denis, C.J.; Van Acker, N.; De Schepper, S.; De Bie, M.; Andries, L.; Fransen, E.; Hendriks, D.; Kockx, M.M.; Lambeir, A.M.
Mapping of carboxypeptidase m in normal human kidney and renal cell carcinoma: expression in tumor-associated neovasculature and macrophages
J. Histochem. Cytochem.
61
218-235
2013
Homo sapiens
brenda
Chu, M.; Wu, S.; Wang, W.; Yu, Y.; Zhang, M.; Sang, L.; Tian, T.; Lu, Y.; Yuan, W.; Huang, Q.; Yi, M.; Gao, Y.; Xiao, J.; Lian, Y.; Zhuang, X.; Zhang, Z.F.; Wu, J.
Functional variant of the carboxypeptidase M (CPM) gene may affect silica-related pneumoconiosis susceptibility by its expression a multistage case-control study
Occup. Environ. Med.
76
169-174
2019
Homo sapiens (P14384)
brenda
Lu, D.; Yao, Q.; Zhan, C.; Le-Meng, Z.; Liu, H.; Cai, Y.; Tu, C.; Li, X.; Zou, Y.; Zhang, S.
MicroRNA-146a promote cell migration and invasion in human colorectal cancer via carboxypeptidase M/src-FAK pathway
Oncotarget
8
22674-22684
2017
Homo sapiens (P14384), Homo sapiens
brenda