Zinc carboxypeptidase

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Zinc carboxypeptidase
Identifiers
SymbolPeptidase_M14
Pfam PF00246
InterPro IPR000834
PROSITE PDOC00123
SCOP2 1cbx / SCOPe / SUPFAM
CDD cd00596
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB 1jqg A:127-412 2c1c A:128-415 1hee E:128-406

2abz A:128-406 1ell P:128-406 1cps :128-406 1bav D:128-406 1m4l A:128-406 1zlh A:128-406 4cpa B:128-406 1hdu D:128-406 7cpa :128-406 1cpx A:128-406 1f57 A:128-406 2ctb :128-406 1arm :128-406 5cpa :128-406 3cpa A:128-406 1ee3 P:128-406 1yme :128-406 1cbx :128-406 1hdq A:128-406 1pyt B:128-406 8cpa :128-406 6cpa :128-406 1iy7 A:128-406 2ctc :128-406 1elm P:128-406 1arl :128-406 2boa B:129-408 1aye A:127-404 1dtd A:127-404 1zg9 C:125-404 1zg8 A:125-404 1z5r A:125-404 1nsa :125-404 1zli A:125-404 1kwm A:125-404 1obr :113-402

1uwy A:28-303 1h8l A:16-291

The carboxypeptidase A family can be divided into two subfamilies: carboxypeptidase H (regulatory) and carboxypeptidase A (digestive). [1] Members of the H family have longer C-termini than those of family A, [2] 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. [1]

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. [1] [3] 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. [1] [4]

Other examples of protein families in this entry include:

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;

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References

  1. 1 2 3 4 Rawlings ND, Barrett AJ (1995). Evolutionary families of metallopeptidases. Meth. Enzymol. Vol. 248. pp. 183–228. doi:10.1016/0076-6879(95)48015-3. ISBN   978-0-12-182149-4. PMID   7674922.
  2. Osterman AL, Grishin NV, Smulevitch SV, Zagnitko OP, Matz MV, Stepanov VM, Revina LP (1992). "Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family". J. Protein Chem. 11 (5): 561–570. doi:10.1007/bf01025034. PMID   1449602. S2CID   22920252.
  3. Lipscomb WN, Rees DC, Lewis M (1983). "Refined crystal structure of carboxypeptidase A at 1.54 A resolution". J. Mol. Biol. 168 (2): 367–387. doi:10.1016/S0022-2836(83)80024-2. PMID   6887246.
  4. Huber R, Guasch A, Coll M, Aviles FX (1992). "Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation". J. Mol. Biol. 224 (1): 141–157. doi:10.1016/0022-2836(92)90581-4. PMID   1548696.
This article incorporates text from the public domain Pfam and InterPro: IPR000834