Choriolysin L
| Choriolysin L | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.66 | ||||||||
| CAS no. | 177529-15-6 | ||||||||
| 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 L (EC 3.4.24.66, teleost hatching enzyme (component), low choriolytic enzyme (LCE)) is an enzyme.[1][2][3][4] 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
- ^ Yasumasu, S.; Iuchi, I.; Yamagami, K. (1988). "Medaka hatching enzyme consists of two kinds of proteases which act cooperatively". Zool. Sci. 5: 191–195.
- ^ Yasumasu, S.; Iuchi, I.; Yamagami, K. (1989). "Isolation and some properties of low choriolytic enzyme (LCE), a component of the hatching enzyme of the teleost, Oryzias latipes". J. Biochem. (Tokyo). 105: 212–218. PMID 2656665.
- ^ Yasumasu, S.; Katow, S.; Hamazaki, T.S.; Iuchi, I.; Yamagami, K. (1992). "Two constituent proteases of a teleostean hatching enzyme: concurrent syntheses and packaging in the same secretory granules in discrete arrangement". Dev. Biol. 149: 349–356. doi:10.1016/0012-1606(92)90290-w. PMID 1730389.
- ^ 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.
External links
- Choriolysin+L at the U.S. National Library of Medicine Medical Subject Headings (MeSH)