3.4.24.52: trimerelysin I
This is an abbreviated version!
For detailed information about trimerelysin I, go to the full flat file.
Reaction
Cleavage of only two bonds His10-/-Leu and Ala14-/-Leu in the insulin B chain =
Synonyms
Hemorrhagic metalloproteinase HR1A, Hemorrhagic proteinase HR1A, HR1A, Metalloproteinase HR1A, metalloproteinase HR1b, Trimeresurus metalloendopeptidase I
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.52 - trimerelysin I
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REACTION DIAGRAM
2-Aminobenzoyl-Ala-Gly-Leu-Ala-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala-2,4-dinitroanilinoethylamide
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peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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?
2-aminobenzoyl-Asn-Ala-Phe-Leu-Ala-2,4-dinitroanilinoethylamide + H2O
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2-Aminobenzoyl-Asn-Ala-Pro-Leu-Ala-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Asn-Ala-Pro + Leu-Ala-2,4-dinitroanilinoethylamide
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peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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?
2-Aminobenzoyl-Gly-Phe-Arg-Leu-Leu-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Gly-Phe-Arg + Leu-Leu-2,4-dinitroanilinoethylamide
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peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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?
2-Aminobenzoyl-Phe-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Phe-Ser-Pro + Met-Leu-2,4-dinitroanilinoethylamide
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peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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?
2-Aminobenzoyl-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Ser-Pro + Met-Leu-2,4-dinitroanilinoethylamide
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peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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?
2-Aminobenzoyl-Thr-Glu-Lys-Leu-Val-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Thr-Glu-Lys + Leu-Val-2,4-dinitroanilinoethylamide
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peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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?
Insulin B-chain derived peptide C + H2O
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i.e. fragment Phe1-Ala14, cleavage site: His10-Leu11, poor substrate
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Metalloproteinase HR1A + H2O
Hydrolyzed metalloproteinase HR1A
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MW 60000, bears autoproteolytic activity which is suppressed by more than 0.005 mM Ca2+ or 0.05 mM EDTA
fragment MW 32000 from COOH-terminus and low MW fragments
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Metalloproteinase HR1B + H2O
Hydrolyzed metalloproteinase HR1B
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MW 60000, bears autoproteolytic activity which is suppressed by more than 5 mM Ca2+ or EDTA
fragment MW 34000 and low MW fragments
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Oxidized insulin B-chain + H2O
Peptide C + peptide D + peptide A + peptide B
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rapid hydrolysis, cleavage sites: Ala14-Leu15 and His10-Leu11, the former bond is more rapidly cleaved than the latter, no cleavage of His5-Leu6
i.e. fragments Phe1-Ala14, Leu15-Ala30, Leu11-Ala14 and Phe1-His10
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casein + H2O
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enzyme form HR1A, very poor substrate for HR1B
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2-aminobenzoyl-Asn-Ala-Pro-Ser-Ala-2,4-dinitroanilinoethylamide, 2-aminobenzoyl-Ala-Thr-Asp-Ile-Val-2,4-dinitroanilinoethylamide, 2-aminobenzoyl-Gly-Phe-Arg-Leu-2,4-dinitroanilinoethylamide, 2-aminobenzoyl-Gly-Phe-Leu-Gly-Pro-2,4-dinitroanilinoethylamide
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additional information
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no substrates are insulin B-chain derived peptide D (fragment Leu15-Ala30)
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additional information
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the major hemorrhagic component in the venom of Trimeresurus flavoviridis
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additional information
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high molecular mass hemorrhagic metalloproteinase
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additional information
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the enzyme shows strong hemorrhagic activity
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additional information
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substrate specificity differs from that of enzyme metalloproteinase HR1b
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additional information
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substrate D-Nbeta-(2-(N-methylamino)benzoyl)-2,3-diaminopropionic acid-glycine-Zaa-Yaa-Xaa-alanine-phenylalanine-proline-(2,4-dinitrophenyl)-lysine-D-arginine-D-arginine. Xaa stands for 19 natural amino acids (excluding cysteine). Yaa stands for 5 natural amino acids (proline, tyrosine, lysine, isoleucine and asparagine). Zaa stands for another 5 amino acids (phenylalanine, alanine, valine, glutamine and arginine). HR1a preferres alanine, histidine, proline, methionine, and tyrosine in descending order at Xaa position and valine and aspartic acid at the Yaa and Zaa positions respectively. measured by fluorescence resonance energy transfer
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