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

Endothiapepsin
Identifiers
EC no.3.4.23.22
CAS no.37205-60-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
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

edit
  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". Protease of Endothia parasitica. Methods Enzymol. Vol. 19. pp. 436–445. doi:10.1016/0076-6879(70)19032-x. ISBN 978-0-12-181881-4.
  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.
edit