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Information on EC 3.4.24.12 - envelysin and Organism(s) Hemicentrotus pulcherrimus and UniProt Accession P91953

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.12 envelysin
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This record set is specific for:
Hemicentrotus pulcherrimus
UNIPROT: P91953 not found.
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The taxonomic range for the selected organisms is: Hemicentrotus pulcherrimus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins of the fertilization envelope and dimethylcasein
Synonyms
envelysin, chymostrypsin, sea urchin embryo hatching enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chorion-digesting proteinase
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chorionase
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chymostrypsin
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Envelysin
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hatching enzyme
HCE
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-
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HE
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-
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HEz
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High choriolytic enzyme
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LCE
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Low choriolytic enzyme
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proteinase, chorion-digesting
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sea urchin embryo hatching enzyme
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sea-urchin-hatching proteinase
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CAS REGISTRY NUMBER
COMMENTARY hide
50812-13-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr + H2O
Ala-Ser-Thr-Thr-Thr-Asn + Tyr-Thr
show the reaction diagram
-
i.e. peptide T, partial cleavage at Asn6-Tyr7
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2
show the reaction diagram
-
i.e. substance P
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
show the reaction diagram
-
i.e. bradykinin, partial cleavage at Pro7-Phe8
-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
show the reaction diagram
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i.e. angiotensin I, partial cleavage at Pro7-Phe8
-
?
fertilization envelope + H2O
?
show the reaction diagram
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enzyme exhibits a unique species specificity, it can not dissolve the fertilization envelope of Anthocidaris crassispina, a species of a neighboring taxonomical family, but can dissolve that of more distantly related species, even if with less efficiency
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-
?
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2 + H2O
?
show the reaction diagram
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i.e. mastoparan, clevage sites: Asn2-Leu3, 100%, Ala7-Ala8, 100%, Ala10-Lys11, 47%, and Lys12-Ile13, 47%
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-
?
insulin
?
show the reaction diagram
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oxidized B chain of insulin cleaved at FVNQ-HLCGSHLVEA-LY-LVCGERGFF-YTPKA
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-
?
neurotensin + H2O
?
show the reaction diagram
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-
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?
physalaemin + H2O
?
show the reaction diagram
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-
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?
snake venom alpha-protease
?
show the reaction diagram
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poor substrate
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-
?
thermolysin + H2O
?
show the reaction diagram
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poor substrate
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-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys + H2O
Tyr-Gly-Gly-Phe + Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
show the reaction diagram
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i.e. dynorphin A(1-13), partial cleavage at Phe4-Leu5
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?
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro + H2O
Tyr-Gly-Gly-Phe + Leu-Arg-Lys-Tyr-Pro
show the reaction diagram
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i.e. beta-neoendorphin, partial cleavage at Phe4-Leu5
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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CaCl2 and KCl or NaCl is required
NH4Cl
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order of activation among monovalent cations: NaCl, KCl, NH4Cl
additional information
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a moderate halophilic enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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acetyl-Pro-Arg-Cys-Gly-Val-Pro-Asp-Val-NH2
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alpha2-Macroglobulin
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chymostatin
Li+
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inhibited by any concentration
pepstatin
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slight
phenylmethylsulfonyl fluoride
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HE_HEMPU
591
0
66126
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66123
x * 66123, calculation from nucleotide sequence
135000
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hatching enzyme secreted from the blastula with the fertilization envelope, gel filtration
80000
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hatching enzyme secreted from the blastula without the fertilization envelope, gel filtration
89000
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intracellular hatching enzyme
additional information
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-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 66123, calculation from nucleotide sequence
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the mature 50000 Da enzyme is highly susceptible to autolytic cleavage at Gln503-Leu504, producing the 38000 Da form retaining catalytic activity and substrate specificity against fertilization envelope
CaCl2 and KCl or NaCl is required for stability
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the enzyme is stabilized by CaCl2, NaCl and KCl. The enzyme is stabilized by dialysis against 1 M NaCl or KCl in the presence of CaCl2
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakatsuka, M.
Properties of intracellular hatching enzyme in the embryos of the sea urchin, Hemicentrotus pulcherrrimus
Dev. Growth Differ.
27
653-661
1985
Hemicentrotus pulcherrimus
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Manually annotated by BRENDA team
Nomura, K.; Tanaka, H.; Kikkawa, Y.; Yamaguchi, M.; Suzuki, N.
The specificity of sea urchin hatching enzyme (envelysin) places it in the mammalian matrix metalloproteinase family
Biochemistry
30
6115-6123
1991
Hemicentrotus pulcherrimus
Manually annotated by BRENDA team
Nomura, K.; Shimizu, T.; Kinoh, H.; Sendai, Y.; Inomata, M.; Suzuki, N.
Sea urchin hatching enzyme (envelysin): cDNA cloning and deprivation of protein substrate specificity by autolytic degradation
Biochemistry
36
7225-7238
1997
Hemicentrotus pulcherrimus (P91953)
Manually annotated by BRENDA team
Nomura, K.; Suzuki, N.
Stereo-specific inhibition of sea urchin envelysin (hatching enzyme) by a synthetic autoinhibitor peptide with a cysteine-switch consensus sequence
FEBS Lett.
321
84-88
1993
Hemicentrotus pulcherrimus
Manually annotated by BRENDA team
Nakatsuka, M.
Salt-dependent properties of hatching enzyme from embryos of the sea urchin, Hemicentrotus pulcherrimus
Dev. Growth Differ.
21
245-253
1979
Hemicentrotus pulcherrimus
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Manually annotated by BRENDA team
Gache, C.; Lepage, T.; Croce, J.; Lhomond, G.
Envelysin
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
575-578
2004
Echinoidea, Hemicentrotus pulcherrimus, Paracentrotus lividus, Strongylocentrotus purpuratus
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Manually annotated by BRENDA team