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Enzyme Nomenclature
Information on EC 3.4.24.66 - choriolysin L
for references in articles please use BRENDA:EC3.4.24.66
Word Map on EC 3.4.24.66
- 3.4.24.66
- fish
- latipes
- oryzias
- zebrafish
- astacin
- rerio
- fundulus
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exon-intron
- heteroclitus
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whole-mount
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teleostean
- salmon
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oviparous
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brachydanio
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astacin-like
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choriogenins
- rockfish
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ovoviviparous
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coregonus
- salar
- masou
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three-spined
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hypoblast
- stickleback
- molecular biology
- degradation
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.24.66
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RECOMMENDED NAME
GeneOntology No.
choriolysin L
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
177529-15-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
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hydrolysis at about 8% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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EVLPLDNPPPA + H2O
EVLPLD + NPPPA
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specific activity: 8.66 nmol/min/microgram protein
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-
?
EVQPPDSPLSI + H2O
EVQPPD + SPLSI
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location: D387/S388 in ChgL (ZI-1,2). Specific activity: 136 nmol/30min/microgram enzyme
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-
?
PGKNPNTPPIG + H2O
PGKNPN + TPPIG
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location: N220/T221 in ChgH (ZI-1,2). Specific activity: 23.9 nmol/30min/microgram enzyme
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-
?
PKLFQDGKPSN + H2O
PKLFQ + DGKPSN
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location: Q136/D137 in ChgH (ZI-1,2). Specific activity: 0.2 nmol/30min/microgram enzyme
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?
PSKRPEAPGVP + H2O
PSKRPE + APGVP
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specific activity: 0.56 nmol/min/microgram protein
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?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
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best substrate of peptidyl 4-methylcoumarin 7-amides
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SVPVVRTSQAA + H2O
SVPVVR + TSQAA
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specific activity: 19.5 nmol/min/microgram protein
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?
VPFELRYPVPA + H2O
VPFELR + YPVPA
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specific activity: 10.36 nmol/min/microgram protein
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?
VPFEQRYPVPA + H2O
VPFEQR + YPVPA
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location: R73/Y74 in ChgL (ZI-3). Specific activity: 76.3 nmol/30min/microgram enzyme
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?
YPSKPQTPTET + H2O
YPSKPQ + TPTET
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specific activity: 2.71 nmol/min/microgram protein
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?
Swollen chorion + H2O
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i.e. inner layer of chorion that has been swollen by previous action of choriolysin H, EC 3.4.24.67, essential reaction in choriolysis, component of embryo-secreted hatching enzyme that digests egg envelope
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additional information
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egg envelope digestion: by electron microscopy it is shown that the egg envelope becomes swollen after treatment with the purified EHE. The EHE cleavage sites on the zona pellucida (ZP) protein of the egg envelope are located in the N-terminal repeat regions
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additional information
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cleavage sites of FHCE and FLCE on egg envelope subunit proteins are determined by comparing the N-terminal amino acid sequences of digests with the sequences deduced from the cDNAs for egg envelope subunit proteins. FHCE and FLCE cleave different sites of the subunit proteins. FLCE cleaves the inside of the zona pellucida domain, the core structure of egg envelope subunit protein, to completely digest the FHCE swollen envelope
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additional information
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unfertilized egg envelope (UFE) is digested by one of the enzymes FHCE1/2 or FLCE
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additional information
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poor substrates are succinyl-Ala-Pro-Ala 4-methylcoumarin 7-amide, succinyl-Ala-Ala-Pro-Phe 4-methylcoumarin 7-amide, N-tert-butoxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide, N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg 4-methylcoumarin 7-amide, N-tert-butoxycarbonyl-Leu-Thr-Arg 4-methylcoumarin 7-amide, N-tert-butoxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide, N-tert-butoxycarbonyl-Val-Leu-Lys 4-methylcoumarin 7-amide, no substrates are intact chorion or Gly-Pro 4-methylcoumarin 7-amide
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additional information
?
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cleavage sites of HCE and LCE on the egg envelope that are primarily constructed of two groups of subunit proteins, ZI-1,2 and ZI-3, are determined. LCE cleaves the middle of the zona pellucida (ZP) domain of ZI-1,2, in addition to the upstream of the trefoil domain of ZI-1,2 and the ZP domain of ZI-3. This middle site is in the intervening sequence connecting two subdomains of the ZP domain. Cleaving this site results in the solubilization of the swollen egg envelope by the disruption of the filamentous structure that is formed by the non-covalent polymerization of ZP domains
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Swollen chorion + H2O
?
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i.e. inner layer of chorion that has been swollen by previous action of choriolysin H, EC 3.4.24.67, essential reaction in choriolysis, component of embryo-secreted hatching enzyme that digests egg envelope
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additional information
?
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egg envelope digestion: by electron microscopy it is shown that the egg envelope becomes swollen after treatment with the purified EHE. The EHE cleavage sites on the zona pellucida (ZP) protein of the egg envelope are located in the N-terminal repeat regions
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Magnesium
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0.00164 mg/mg protein, inductively coupled plasma emission analysis
Zinc
Zn2+
additional information
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no cobalt, manganese or iron detected by inductively coupled plasma emission analysis
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
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0.5 mM, choriolytic and caseinolytic activity, 1 mM Zn2+ restores, 5 mM Cu2+ partially restores, not Ca2+ or Mg2+
additional information
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no inhibition of caseinolytic activity by 1-10 mM IAA, monoiodoacetic acid or diisopropyl fluorophosphate
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additional information
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not inhibited by DFP, iodoacetamide or iodoacetic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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in stage 25 embryos, strong expression of LCE found in branchial arches
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in stage 19 embryos, LCE gene transcripts detected in a U-shaped cell mass at the anterior of the forebrain
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i.e. culture medium of blastulae; taken immediately after larvae hatched on the 6th day
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25500
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
inserted into a pGEM-T easy vector, cloning of full-length c-DNA by 5'- and 3'-RACE method
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single copy of MLCE gene, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparison and phylogenetic analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
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first choriolysin H swells the inner layer of egg envelope by limited digestion, and then choriolysin L solubilizes the swollen part of it completely
molecular biology
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putative embryonic seCL148 product is most closely related to medaka choriolysin L
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.24.66)
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