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by | Mar 16, 2018 | Hosta

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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

  1. ^ Blundell TL, Jenkins JA, Sewell BT, Pearl LH, Cooper JB, Tickle IJ, Veerapandian B, Wood SP (February 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.
  2. ^ Hemmings AM, Foundling SI, Sibanda BL, Wood SP, Pearl LH, Blundell T (December 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.
  3. ^ Whitaker, J.R. (1970). "Protease of Endothia parasitica". Methods Enzymol. 19: 436–445. doi:10.1016/0076-6879(70)19032-x.
  4. ^ Williams DC, Witaker JR, Caldwell PV (March 1972). "Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease". Archives of Biochemistry and Biophysics. 149 (1): 52–61. doi:10.1016/0003-9861(72)90298-6. PMID 4552802.
  5. ^ Barkholt V (September 1987). "Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica". European Journal of Biochemistry. 167 (2): 327–38. doi:10.1111/j.1432-1033.1987.tb13340.x. PMID 3305016.
  6. ^ Cooper J, Foundling S, Hemmings A, Blundell T, Jones DM, Hallett A, Szelke M (November 1987). "The structure of a synthetic pepsin inhibitor complexed with endothiapepsin". European Journal of Biochemistry. 169 (1): 215–21. doi:10.1111/j.1432-1033.1987.tb13600.x. PMID 3119339.

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