Carboxypeptidase M

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Carboxypeptidase M
Carboxypeptidase M
Identifiers
EC no.	3.4.17.12
CAS no.	120038-28-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

CPM
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1UWY
Identifiers
Aliases	CPM, carboxypeptidase M, Carboxypeptidase M
External IDs	OMIM: 114860; MGI: 1917824; HomoloGene: 35367; GeneCards: CPM; OMA:CPM - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	68,971,570 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	117,523,257 bp
RNA expression pattern
	Top expressed in
	lower lobe of lung; ; subcutaneous adipose tissue; ; right lung; ; visceral pleura; ; mucosa of sigmoid colon; ; rectum; ; abdominal fat; ; placenta; ; upper lobe of lung; ; corpus callosum;
	Top expressed in
	left lung lobe; ; seminal vesicula; ; lumbar subsegment of spinal cord; ; vestibular membrane of cochlear duct; ; right lung lobe; ; olfactory system; ; olfactory epithelium; ; skin of external ear; ; hand; ; lip;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	carboxypeptidase activity; peptidase activity; zinc ion binding; hydrolase activity; metallopeptidase activity; metal ion binding; metallocarboxypeptidase activity; serine-type carboxypeptidase activity;
Cellular component	anchored component of membrane; cell surface; plasma membrane; extracellular exosome; membrane; extracellular region; extracellular space;
Biological process	protein processing; anatomical structure morphogenesis; proteolysis; peptide metabolic process; C-terminal protein lipidation;
	Sources:Amigo / QuickGO
Orthologs
	1368
	70574
	ENSG00000135678
	ENSMUSG00000020183
	P14384
	Q80V42
	NM_001005502; NM_001874; NM_198320
	NM_027468
	NP_001005502; NP_001865; NP_938079
	NP_081744
	Wikidata
View/Edit Human	View/Edit Mouse

Carboxypeptidase M (EC 3.4.17.12) is an enzyme that in humans is encoded by the CPM gene.^[5]^[6]^[7]^[8]^[9]

Function

Carboxypeptidase M is a membrane-bound arginine/lysine carboxypeptidase. This enzyme catalyses cleavage of C-terminal arginine or lysine residues from polypeptides. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000135678 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020183 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Kas K, Schoenmakers EF, Van de Ven WJ (November 1995). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics. 30 (2): 403–5. PMID 8586455.
^ ^a ^b "Entrez Gene: CPM carboxypeptidase M".
^ Skidgel RA (August 1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends in Pharmacological Sciences. 9 (8): 299–304. doi:10.1016/0165-6147(88)90015-6. PMID 3074547.
^ Deddish PA, Skidgel RA, Erdös EG (July 1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)". The Biochemical Journal. 261 (1): 289–91. doi:10.1042/bj2610289. PMC 1138816. PMID 2775217.
^ Skidgel RA, Davis RM, Tan F (February 1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones". The Journal of Biological Chemistry. 264 (4): 2236–41. doi:10.1016/S0021-9258(18)94167-0. PMID 2914904.

External links

Carboxypeptidase+M at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Human CPM genome location and CPM gene details page in the UCSC Genome Browser.

Fujiwara H, Imai K, Inoue T, Maeda M, Fujii S (February 1999). "Membrane-bound cell surface peptidases in reproductive organs". Endocrine Journal. 46 (1): 11–25. doi:10.1507/endocrj.46.11. PMID 10426564.
Rehli M, Krause SW, Andreesen R (2000). "The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo". Cellular Peptidases in Immune Functions and Diseases 2. Advances in Experimental Medicine and Biology. Vol. 477. pp. 205–16. doi:10.1007/0-306-46826-3_23. ISBN 0-306-46383-0. PMID 10849748.
Nagae A, Deddish PA, Becker RP, Anderson CH, Abe M, Tan F, Skidgel RA, Erdös EG (December 1992). "Carboxypeptidase M in brain and peripheral nerves". Journal of Neurochemistry. 59 (6): 2201–12. doi:10.1111/j.1471-4159.1992.tb10112.x. PMID 1431901. S2CID 19152354.
Tan F, Chan SJ, Steiner DF, Schilling JW, Skidgel RA (August 1989). "Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N". The Journal of Biological Chemistry. 264 (22): 13165–70. doi:10.1016/S0021-9258(18)51610-0. PMID 2753907.
Skidgel RA, Davis RM, Tan F (February 1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones". The Journal of Biological Chemistry. 264 (4): 2236–41. doi:10.1016/S0021-9258(18)94167-0. PMID 2914904.
McGwire GB, Skidgel RA (July 1995). "Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M". The Journal of Biological Chemistry. 270 (29): 17154–8. doi:10.1074/jbc.270.29.17154. PMID 7615511.
de Saint-Vis B, Cupillard L, Pandrau-Garcia D, Ho S, Renard N, Grouard G, Duvert V, Thomas X, Galizzi JP, Banchereau J (August 1995). "Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13". Blood. 86 (3): 1098–105. doi:10.1182/blood.V86.3.1098.1098. PMID 7620164.
Rehli M, Krause SW, Kreutz M, Andreesen R (June 1995). "Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation". The Journal of Biological Chemistry. 270 (26): 15644–9. doi:10.1074/jbc.270.26.15644. PMID 7797563.
Nagae A, Abe M, Becker RP, Deddish PA, Skidgel RA, Erdös EG (August 1993). "High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells". American Journal of Respiratory Cell and Molecular Biology. 9 (2): 221–9. doi:10.1165/ajrcmb/9.2.221. PMID 8338689.
Michel B, Igić R, Leray V, Deddish PA, Erdös EG (April 1996). "Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M". Circulation Research. 78 (4): 635–42. doi:10.1161/01.res.78.4.635. PMID 8635221.
Skidgel RA, McGwire GB, Li XY (May 1996). "Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones". Immunopharmacology. 32 (1–3): 48–52. doi:10.1016/0162-3109(96)00008-2. PMID 8796265.
Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Yoshioka S, Fujiwara H, Yamada S, Nakayama T, Higuchi T, Inoue T, Mori T, Maeda M (July 1998). "Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy". Molecular Human Reproduction. 4 (7): 709–17. doi:10.1093/molehr/4.7.709. PMID 9701794.
Li XY, Skidgel RA (April 1999). "Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis". Biochemical and Biophysical Research Communications. 258 (1): 204–10. doi:10.1006/bbrc.1999.0619. PMID 10222261.
Bektas A, Hughes JN, Warram JH, Krolewski AS, Doria A (January 2001). "Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes". Diabetes. 50 (1): 204–8. doi:10.2337/diabetes.50.1.204. PMID 11147789.
Suzuki Y, Taira H, Tsunoda T, Mizushima-Sugano J, Sese J, Hata H, Ota T, Isogai T, Tanaka T, Morishita S, Okubo K, Sakaki Y, Nakamura Y, Suyama A, Sugano S (May 2001). "Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites". EMBO Reports. 2 (5): 388–93. doi:10.1093/embo-reports/kve085. PMC 1083880. PMID 11375929.
Lendeckel U, Arndt M, Wrenger S, Nepple K, Huth C, Ansorge S, Klein HU, Goette A (June 2001). "Expression and activity of ectopeptidases in fibrillating human atria". Journal of Molecular and Cellular Cardiology. 33 (6): 1273–81. doi:10.1006/jmcc.2001.1389. PMID 11444929.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000135678 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020183 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8586455-5] Kas K, Schoenmakers EF, Van de Ven WJ (November 1995). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics. 30 (2): 403–5. PMID 8586455.

[entrez-6] "Entrez Gene: CPM carboxypeptidase M".

[7] Skidgel RA (August 1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends in Pharmacological Sciences. 9 (8): 299–304. doi:10.1016/0165-6147(88)90015-6. PMID 3074547.

[8] Deddish PA, Skidgel RA, Erdös EG (July 1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)". The Biochemical Journal. 261 (1): 289–91. doi:10.1042/bj2610289. PMC 1138816. PMID 2775217.

[9] Skidgel RA, Davis RM, Tan F (February 1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones". The Journal of Biological Chemistry. 264 (4): 2236–41. doi:10.1016/S0021-9258(18)94167-0. PMID 2914904.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

References

External links

Further reading