EC 3.4.23.22 - Endothiapepsin

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IntEnz Enzyme Nomenclature
EC 3.4.23.22

Names

Accepted name:
endothiapepsin
Other names:
Endothia parasitica acid proteinase
Endothia parasitica aspartic proteinase
Endothia acid proteinase
Endothia aspartic proteinase
Systematic name:
-

Reaction

Comments:

From the ascomycete Endothia parasitica. In peptidase family A1 (pepsin A family). Formerly EC 3.4.23.10, and included in EC 3.4.23.6.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00128
Structural data: CSA , EC2PDB
CAS Registry Number: 37205-60-0
UniProtKB/Swiss-Prot:

References

  1. Whitaker, J.R.
    Protease of Endothia parasitica.
    Methods Enzymol. 19: 436-445 (1970).
  2. Williams, D.C., Whitaker, J.R. and Caldwell, P.V.
    Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease.
    Arch. Biochem. Biophys. 149: 52-61 (1972). [PMID: 4552802]
  3. Barkholt, V.
    Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica.
    Eur. J. Biochem. 167: 327-338 (1987). [PMID: 3305016]
  4. Cooper, J., Foundling, S., Hemmings, A., Blundell, T., Jones, D.M., Hallett, A. and Szelke, M.
    The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
    Eur. J. Biochem. 167: 215-221 (1987). [PMID: 3119339]

[EC 3.4.23.22 created 1992 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992)]