Endothiapepsin
| Endothiapepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.22 | ||||||||
| CAS number | 37205-60-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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.; 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.; 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.
External links
- Endothiapepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/18/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.