Endothiapepsin
      
Endothiapepsin (EC 3.4.23.22, Endothia aspartic proteinase, Endothia acid proteinase, Endothia parasitica acid proteinase, Endothia parasitica aspartic proteinase) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical 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
 
This enzyme is isolated from the ascomycete Endothia parasitica.
 References 
- ↑  Blundell, T. L.; Jenkins, J. A.; Sewell, B. T.; Pearl, L. H.; Cooper, J. B.; Tickle, I. J.; Veerapandian, B; Wood, S. P. (1990). "X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 a resolution of endothiapepsin". Journal of Molecular Biology 211 (4): 919–41. doi:10.1016/0022-2836(90)90084-Y. PMID 2179568. 
 - ↑  Hemmings, A. M.; Foundling, S. I.; Sibanda, B. L.; Wood, S. P.; Pearl, L. H.; Blundell, T (1985). "Energy calculations on aspartic proteinases: Human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142". Biochemical Society Transactions 13 (6): 1036–41. doi:10.1042/bst0131036. PMID 3912234. 
 - ↑  Whitaker, J.R. (1970). "Protease of Endothia parasitica". Methods Enzymol. 19: 436–445. doi:10.1016/0076-6879(70)19032-x. 
 - ↑  Williams, D.C., Whitaker, J.R. and Caldwell, P.V. (1972). "Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease". Arch. Biochem. Biophys. 149: 52–61. doi:10.1016/0003-9861(72)90298-6. PMID 4552802. 
 - ↑  Barkholt, V. (1987). "Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica". Eur. J. Biochem. 167: 327–338. doi:10.1111/j.1432-1033.1987.tb13340.x. PMID 3305016. 
 - ↑  Cooper, J., Foundling, S., Hemmings, A., Blundell, T., Jones, D.M., Hallett, A. and Szelke, M. (1987). "The structure of a synthetic pepsin inhibitor complexed with endothiapepsin". Eur. J. Biochem. 169: 215–221. doi:10.1111/j.1432-1033.1987.tb13600.x. PMID 3119339. 
 
 
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