| 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 3119339] |
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| [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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