Carboxypeptidase A2

CPA2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1AYE, 1DTD, 1O6X
Identifiers
Aliases	CPA2, carboxypeptidase A2
External IDs	OMIM: 600688; MGI: 3617840; HomoloGene: 37541; GeneCards: CPA2; OMA:CPA2 - orthologs
Gene location (Human)
Chr.	Chromosome 7 (human)
End	130,289,798 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	30,564,475 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; islet of Langerhans; ; pancreatic epithelial cell; ; body of stomach; ; beta cell; ; duodenum; ; testicle; ; C1 segment; ; fundus; ; jejunal mucosa;
	Top expressed in
	pyloric antrum; ; islet of Langerhans; ; embryo; ; duodenum; ; retinal pigment epithelium; ; genital tubercle; ; saccule; ; sexually immature organism; ; migratory enteric neural crest cell; ; embryo;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	carboxypeptidase activity; metallopeptidase activity; zinc ion binding; peptidase activity; hydrolase activity; metallocarboxypeptidase activity; metal ion binding;
Cellular component	extracellular region; vacuole; extracellular space;
Biological process	proteolysis; protein catabolic process in the vacuole;
	Sources:Amigo / QuickGO
Orthologs
	1358
	232680
	ENSG00000158516
	ENSMUSG00000071553
	P48052
	Q504N0
	NM_001869
	NM_001024698
	NP_001860
	NP_001019869
	Wikidata
View/Edit Human	View/Edit Mouse

Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene.^[5]^[6]^[7]

Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. The A2 form of pancreatic procarboxypeptidase acts on aromatic C-terminal residues^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000158516 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000071553 – 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.
^ Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M (Apr 1995). "The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model". J Biol Chem. 270 (12): 6651–7. doi:10.1074/jbc.270.12.6651. PMID 7896805.
^ Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T (Aug 2000). "Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32". Genomics. 66 (2): 221–5. doi:10.1006/geno.2000.6206. PMID 10860668.
^ ^a ^b "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)".

External links

The MEROPS online database for peptidases and their inhibitors: M14.002
Overview of all the structural information available in the PDB for UniProt: P48052 (Human Carboxypeptidase A2) at the PDBe-KB.

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000158516 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000071553 – 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.

[pmid7896805-5] Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M (Apr 1995). "The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model". J Biol Chem. 270 (12): 6651–7. doi:10.1074/jbc.270.12.6651. PMID 7896805.

[pmid10860668-6] Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T (Aug 2000). "Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32". Genomics. 66 (2): 221–5. doi:10.1006/geno.2000.6206. PMID 10860668.

[entrez-7] "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)".

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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)

Carboxypeptidase A2

Carboxypeptidase A2

Carboxypeptidase A2

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Carboxypeptidase A2

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