The Enzyme Database

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EC 3.4.23.22     
Accepted name: endothiapepsin
Reaction: Hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1′, but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
Other name(s): Endothia aspartic proteinase; Endothia acid proteinase; Endothia parasitica acid proteinase; Endothia parasitica aspartic proteinase
Comments: From the ascomycete Endothia parasitica. In peptidase family A1 (pepsin A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 37205-60-0
References:
1.  Whitaker, J.R. Protease of Endothia parasitica. Methods Enzymol. 19 (1970) 436–445.
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 (1972) 52–61. [PMID: 4552802]
3.  Barkholt, V. Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica. Eur. J. Biochem. 167 (1987) 327–338. [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. 169 (1987) 215–221. [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)]
 
 


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