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Literature summary extracted from

  • 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 (1991), Biochemistry, 30, 6115-6123.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.12 1,10-phenanthroline
-
Hemicentrotus pulcherrimus
3.4.24.12 alpha2-Macroglobulin
-
Hemicentrotus pulcherrimus
3.4.24.12 chymostatin slight Hemicentrotus pulcherrimus
3.4.24.12 EDTA
-
Hemicentrotus pulcherrimus
3.4.24.12 EGTA
-
Hemicentrotus pulcherrimus
3.4.24.12 pepstatin slight Hemicentrotus pulcherrimus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.12 Hemicentrotus pulcherrimus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.12
-
Hemicentrotus pulcherrimus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.12 hatching liquid
-
Hemicentrotus pulcherrimus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.12 Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr + H2O i.e. peptide T, partial cleavage at Asn6-Tyr7 Hemicentrotus pulcherrimus Ala-Ser-Thr-Thr-Thr-Asn + Tyr-Thr
-
?
3.4.24.12 Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O i.e. substance P Hemicentrotus pulcherrimus Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly-Leu-Met-NH2
-
?
3.4.24.12 Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O i.e. bradykinin, partial cleavage at Pro7-Phe8 Hemicentrotus pulcherrimus Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
?
3.4.24.12 Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O i.e. angiotensin I, partial cleavage at Pro7-Phe8 Hemicentrotus pulcherrimus Asp-Arg-Val-Tyr-Ile-His-Pro + Phe-His-Leu
-
?
3.4.24.12 fertilization envelope + H2O 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 Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2 + H2O i.e. mastoparan, clevage sites: Asn2-Leu3, 100%, Ala7-Ala8, 100%, Ala10-Lys11, 47%, and Lys12-Ile13, 47% Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 additional information preferentially cleaves the peptide bond on the amino side of bulky hydrophobic residues, -Leu, -Ile, and -Phe as well as -Tyr Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 neurotensin + H2O
-
Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 physalaemin + H2O
-
Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 snake venom alpha-protease poor substrate Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 thermolysin + H2O poor substrate Hemicentrotus pulcherrimus ?
-
?
3.4.24.12 Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys + H2O i.e. dynorphin A(1-13), partial cleavage at Phe4-Leu5 Hemicentrotus pulcherrimus Tyr-Gly-Gly-Phe + Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
?
3.4.24.12 Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro + H2O i.e. beta-neoendorphin, partial cleavage at Phe4-Leu5 Hemicentrotus pulcherrimus Tyr-Gly-Gly-Phe + Leu-Arg-Lys-Tyr-Pro
-
?