CPM - Carboxypeptidase M - human protein (Function)
 
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CPM »  Carboxypeptidase M   [ EC 3.4.17.12 ]  (CPM)
 
Gene name:  CPM
Family name: Peptidase M14
Entry whose protein(s) existence is based on evidence at protein level
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Function

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Overview 
Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.  
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  • UniProtKB
GO molecular function 
Carboxypeptidase activitydefinition[GO:0004180]  
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  • PINC
Metallocarboxypeptidase activitydefinition[GO:0004181] silver  
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  • InterPro 2 GO
Zinc ion bindingdefinition[GO:0008270] silver  
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  • InterPro 2 GO
GO biological process 
Anatomical structure morphogenesisdefinition[GO:0009653]  
1
  • PINC
Proteolysisdefinition[GO:0006508]  
1
  • UniProtKB KW
Enzymatic activity 
This protein acts as an enzyme. It is known to catalyze the following reaction
EC 3.4.17.12: Cleavage of C-terminal arginine or lysine residues from polypeptides.  
1
  • UniProtKB
It requires the following cofactor
 Zn(2+) : Binds 1 zinc ion per subunit.  
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  • UniProtKB
It is regulated in the following manner
Inhibited by O-phenanthroline and MGTA and activated by cobalt.  
1
  • UniProtKB
 
More information is available from:
 

Biophysicochemical properties

Kinetic parameters
KM 57 uM for placental peptide hormones
KM 59 uM for synthetic dansyl-Ala-Arg
Dependence
pH Optimum pH is 7.0.

Keywords

Molecular function 
Carboxypeptidase  definition   [KW-0121]
Hydrolase  definition   [KW-0378]
Metalloprotease  definition   [KW-0482]
Protease  definition   [KW-0645]
Technical term 
Reference proteome  definition   [KW-1185]
 

Further external links

Enzyme and pathway databases
SABIO-RK: P14384
Other
GeneWiki: CPM_(gene)
GenomeRNAi: 1368
PRO: PR:P14384