Choriolysin L
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
Choriolysin L | |||||||||
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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 | ||||||||
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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". Zoological Science. 5: 191–195.
- Yasumasu S, Iuchi I, Yamagami K (February 1989). "Isolation and some properties of low choriolytic enzyme (LCE), a component of the hatching enzyme of the teleost, Oryzias latipes". Journal of Biochemistry. 105 (2): 212–8. doi:10.1093/oxfordjournals.jbchem.a122641. PMID 2656665.
- Yasumasu S, Katow S, Hamazaki TS, Iuchi I, Yamagami K (February 1992). "Two constituent proteases of a teleostean hatching enzyme: concurrent syntheses and packaging in the same secretory granules in discrete arrangement". Developmental Biology. 149 (2): 349–56. doi:10.1016/0012-1606(92)90290-w. PMID 1730389.
- Yasumasu S, Yamada K, Akasaka K, Mitsunaga K, Iuchi I, Shimada H, Yamagami K (October 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". Developmental Biology. 153 (2): 250–8. 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)
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