Choriolysin H
| Choriolysin H | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.67 | ||||||||
| CAS no. | 177529-16-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Choriolysin H (EC 3.4.24.67, teleost hatching enzyme (component), high choriolytic enzyme (HCE)) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-7-(4-methyl)coumarylamide
This enzyme is present in teleost fish Oryzias latipes.
References
- ^ Yamagami, K. (1972). "Isolation of a choriolytic enzyme (hatching enzyme) of the teleost, Oryzias latipes". Dev. Biol. 29: 343–348. doi:10.1016/0012-1606(72)90074-7. PMID 4652273.
- ^ Yasumasu, S.; Iuchi, I.; Yamagami, K. (1989). "Purification and partial characterization of high choriolytic enzyme (HCE), a component of the hatching enzyme of the teleost, Oryzias latipes". J. Biochem. (Tokyo). 105: 204–211. PMID 2656664.
- ^ Yasumasu, S.; Katow, S.; Umino, Y.; Iuchi, I.; Yamagami, K. (1989). "A unique proteolytic action of HCE, a constituent protease of a fish hatching enzyme: tight binding to its natural substrate, egg envelope". Biochem. Biophys. Res. Commun. 162: 58–63. doi:10.1016/0006-291x(89)91961-x. PMID 2751672.
- ^ Yasumasu, S.; Yamada, K.; Akasaka, K.; Mitsunaga, K.; Iuchi, I.; Shimada, H.; Yamagami, K. (1992). "Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development". Dev. Biol. 153: 250–258. doi:10.1016/0012-1606(92)90110-3. PMID 1397682.
- ^ Lee, K.S.; Yasumasu, S.; Nomura, K.; Iuchi, I. (1993). "HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion". FEBS Lett. 339: 281–284. doi:10.1016/0014-5793(94)80431-1. PMID 8112467.
External links
- Choriolysin+H at the U.S. National Library of Medicine Medical Subject Headings (MeSH)