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Information on EC 3.4.24.66 - choriolysin L for references in articles please use BRENDA:EC3.4.24.66Word Map on EC 3.4.24.66
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The enzyme appears in viruses and cellular organisms
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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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hydrolysis of peptide bond
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EHE
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contains several isoenzymes
embryo-specific hatching enzyme
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medaka hatching enzyme
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medaka low choriolytic enzyme
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Teleost hatching enzyme (component)
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LCE
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Low choriolytic enzyme
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Low choriolytic enzyme
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Low choriolytic enzyme
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additional information
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homologue of astacin
additional information
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the enzyme is an astacin family zinc endopeptidase
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medaka, teleost fish, orange-red variety
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orange-red variety of medaka
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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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GSKGSDETFH + H2O
GSKGS + DETFH
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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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RPTFGRPGIT + H2O
RPTFG + RPGIT
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RPTIGRPGFT + H2O
RPTIG + RPGFT
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RPTLGEPTHT + H2O
RPTLG + EPTHT
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RPTLGGPKGS + H2O
RPTLG + GPKGS
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Suc-Leu-Leu-Val-Tyr-4-methylcoumarin-7-amide + H2O
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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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additional information
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casein + H2O
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chorion + H2O
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synergetic digestion by HCE and LCE
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chorion + H2O
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Swollen chorion + H2O
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Swollen chorion + H2O
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i.e. partially digested chorion
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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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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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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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Calcium
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0.00538 mg/mg protein, inductively coupled plasma emission analysis
Cu2+
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partly reactivates EDTA-inactivated apoenzyme
Magnesium
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0.00164 mg/mg protein, inductively coupled plasma emission analysis
additional information
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no cobalt, manganese or iron detected by inductively coupled plasma emission analysis
Zinc
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0.00124 mg/mg protein, inductively coupled plasma emission analysis
Zn2+
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reactivates EDTA-inactivated apoenzyme
Zn2+
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zinc endopeptidase
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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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EVQPPDSPLSI
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pH 8.0, 30°C
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additional information
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8.5
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caseinolytic activity
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for caseinolytic activity
additional information
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pI: 9.8
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assay at
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7 - 9
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about 50% of maximal caseinolytic activity at pH 6.5 and 8.9
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assay at
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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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prehatching embryo, 3 days old, embryo-secreted enzyme
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the enzyme is expressed only in pre-hatching embryos
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colocalized with choriolysin H in the secretory granules
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i.e. culture medium of blastulae; taken immediately after larvae hatched on the 6th day
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i.e. culture medium of blastulae
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at the periphery, immunocytochemical detection
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23100
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Oryzias latipes, deduced from nucleotide sequence
additional information
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amino acid composition
25500
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1 * 25500, Oryzias latipes, SDS-PAGE
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1 * 25500, Oryzias latipes, SDS-PAGE
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partly purified by gel filtration and cation-exchange column
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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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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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LCE_ORYLA
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30985
Swiss-Prot
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Yasumasu, S.; Iuchi, I.; Yamagami, K.
Isolation and some properties of low choriolytic enzyme (LCE), a component of the hatching enzyme of the teleost, Oryzias latipes
J. Biochem.
105
212-218
1989
Oryzias latipes
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Yasumasu, S.; Katow, S.; Hamazaki, T.S.; Iuchi, I.; Yamagami, K.
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
1992
Oryzias latipes
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Yasumasu, S.; Yamada, K.; Akasaka, K.; Mitsunaga, K.; Iuchi, I.; Shimada, H.; Yamagami, K.
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
1992
Oryzias latipes
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Kawaguchi, M.; Yasumasu, S.; Shimizu, A.; Hiroi, J.; Yoshizaki, N.; Nagata, K.; Tanokura, M.; Iuchi, I.
Purification and gene cloning of Fundulus heteroclitus hatching enzyme. A hatching enzyme system composed of high choriolytic enzyme and low choriolytic enzyme is conserved between two different teleosts, Fundulus heteroclitus and medaka Oryzias latipes
FEBS J.
272
4315-4326
2005
Fundulus heteroclitus
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Donato, D.M.; Hiramatsu, N.; Arey, K.M.; Hiramatsu, K.; Kennedy, A.M.; Morton, C.L.; Hara, A.; Sullivan, C.V.
Atresia in temperate basses: cloning of hatching enzyme (choriolysin) homologues from atretic ovaries
Fish Physiol. Biochem.
28
329-330
2004
Morone saxatilis
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brenda
Yasumasu, S.; Yamagami, K.
Choriolysin L
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
623-625
2004
Oryzias latipes
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brenda
Kawaguchi, M.; Yasumasu, S.; Hiroi, J.; Naruse, K.; Inoue, M.; Iuchi, I.
Evolution of teleostean hatching enzyme genes and their paralogous genes
Dev. Genes Evol.
216
769-784
2006
Oryzias latipes
brenda
Kawaguchi, M.; Yasumasu, S.; Shimizu, A.; Sano, K.; Iuchi, I.; Nishida, M.
Conservation of the egg envelope digestion mechanism of hatching enzyme in euteleostean fishes
FEBS J.
277
4973-4987
2010
Fundulus heteroclitus
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Sano, K.; Kawaguchi, M.; Yoshikawa, M.; Kaneko, T.; Tanaka, T.; Iuchi, I.; Yasumasu, S.
Hatching enzyme of Japanese eel Anguilla japonica and the possible evolution of the egg envelope digestion mechanism
FEBS J.
278
3711-3723
2011
Anguilla japonica
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Yasumasu, S.; Kawaguchi, M.; Ouchi, S.; Sano, K.; Murata, K.; Sugiyama, H.; Akema, T.; Iuchi, I.
Mechanism of egg envelope digestion by hatching enzymes, HCE and LCE in medaka, Oryzias latipes
J. Biochem.
148
439-448
2010
Oryzias latipes
brenda
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