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
Search PMC articles PubMed articles NCBI proteins

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

1. Yasumasu S, Iuchi I, Yamagami K (1988). "Medaka hatching enzyme consists of two kinds of proteases which act cooperatively". Zoological Science. 5: 191–195.
2. 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.
3. 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.
4. 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)