Zinc carboxypeptidase

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]

Zinc carboxypeptidase
Identifiers
SymbolPeptidase_M14
PfamPF00246
InterProIPR000834
PROSITEPDOC00123
SCOPe1cbx / SUPFAM
CDDcd00596

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:

  • 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;

gollark: You're going to have a TOML binding file like this:```tomlfile = "io.o"[io][io.putchar]name = "io_putchar"args = 1[io.putint]name = "io_putint"args = 1```declaring functions from an object file.
gollark: Apparently Aidan is implementing RPNCalc to x86 FFI capability.
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References
  1. Rawlings ND, Barrett AJ (1995). "Evolutionary families of metallopeptidases". Meth. Enzymol. 248: 183–228. doi:10.1016/0076-6879(95)48015-3. 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.
  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
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