KEGG   ENZYME: 3.4.24.67Help
Entry
EC 3.4.24.67                Enzyme                                 

Name
choriolysin H;
teleost hatching enzyme (component);
high choriolytic enzyme (HCE)
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
Comment
Known from the teleost fish Oryzias latipes (medaka). Efficient dissolution of the egg membrane requires concerted action with choriolysin L. A 25.5 kDa peptidase in family M12 (astacin family)
History
EC 3.4.24.67 created 1995
Orthology
K18543  
choriolysin H
Genes
DRE: 
407971(he1b)
TRU: 
MZE: 
OLA: 
SASA: 
Taxonomy
Reference
1  [PMID:4652273]
  Authors
Yamagami K.
  Title
Isolation of a choriolytic enzyme (hatching enzyme) of the teleost, Oryzias latipes.
  Journal
Dev. Biol. 29 (1972) 343-8.
Reference
2  [PMID:2656664]
  Authors
Yasumasu S, Iuchi I, Yamagami K.
  Title
Purification and partial characterization of high choriolytic enzyme (HCE), a component of the hatching enzyme of the teleost, Oryzias latipes.
  Journal
J. Biochem. (Tokyo). 105 (1989) 204-11.
Reference
3  [PMID:2751672]
  Authors
Yasumasu S, Katow S, Umino Y, Iuchi I, Yamagami K.
  Title
A unique proteolytic action of HCE, a constituent protease of a fish hatching enzyme: tight binding to its natural substrate, egg envelope.
  Journal
Biochem. Biophys. Res. Commun. 162 (1989) 58-63.
Reference
4  [PMID:1397682]
  Authors
Yasumasu S, Yamada K, Akasaka K, Mitsunaga K, Iuchi I, Shimada H, Yamagami K.
  Title
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.
  Journal
Dev. Biol. 153 (1992) 250-8.
  Sequence
Reference
5  [PMID:8112467]
  Authors
Lee KS, Yasumasu S, Nomura K, Iuchi I.
  Title
HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion.
  Journal
FEBS. Lett. 339 (1994) 281-4.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
177529-16-7

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