Harman Patil (Editor)

Zinc carboxypeptidase

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Symbol
  
Peptidase_M14

InterPro
  
IPR000834

SCOP
  
1cbx

Pfam
  
PF00246

PROSITE
  
PDOC00123

SUPERFAMILY
  
1cbx

The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). Members of the H family have longer C-termini than those of family A, and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble.

The zinc ligands have been determined as two histidines and a glutamate, and the catalytic residue has been identified as a C-terminal glutamate, but these do not form the characteristic metalloprotease HEXXH motif. Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended alpha-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts.

Other examples of protein families in this entry include:

  • Intron maturase
  • Putative mitochondrial processing peptidase alpha subunit
  • Superoxide dismutase [Mn] (EC 1.15.1.1)
  • Asparagine synthetase [glutamine-hydrolysing] 3 (EC 6.3.5.4)
  • Glucose-6-phosphate isomerase (EC 5.3.1.9)
  • Human proteins containing this domain

    AEBP1; AGBL1; AGBL2; AGBL3; AGBL4; AGBL5; AGTPBP1; CPA1; CPA2; CPA3; CPA4; CPA5; CPA6; CPB1; CPB2; CPD; CPE; CPM; CPN1; CPO; CPXM1; CPXM2; CPZ;

    References

    Zinc carboxypeptidase Wikipedia


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