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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 + H2O
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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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additional information
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casein + H2O
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casein + H2O
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enzyme form HR1A, very poor substrate for HR1B
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additional information
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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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Omori-Satoh, T.; Sadahiro, S.
Resolution of the major hemorrhagic component of Trimeresurus flavoviridis venom into two parts
Biochim. Biophys. Acta
580
392-404
1979
Protobothrops flavoviridis
brenda
Yamakawa, Y.; Omori-Satoh, T.
The sites of cleavage in oxidized insulin-B chain by a hemorrhagic protease derived from the venom of the habu (Trimeresurus flavoviridis)
Toxicon
26
227-231
1988
Protobothrops flavoviridis
brenda
Takeya, H.; Oda, K.; Miyata, T.; Omori-Satoh, T.; Iwanaga, S.
The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis
J. Biol. Chem.
265
16068-16073
1990
Protobothrops flavoviridis
brenda
Takeya, H.; Nishida, S.; Nishino, N.; Makinose, Y.; Omori-Satoh, T.; Nikai, T.; Sugihara, H.; Iwanaga, S.
Primary structures of platelet aggregation inhibitors (disintegrins) autoproteolytically released from snake venom hemorrhagic metalloproteinases and new fluorogenic peptide substrates for these enzymes
J. Biochem.
113
473-483
1993
Protobothrops flavoviridis
brenda
Kawabata, S.; Iwanaga, S.
Trimerelysin I
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
702-703
2004
Protobothrops flavoviridis
-
brenda
Morine, N.; Matsuda, S.; Terada, K.; Eto, A.; Ishida, I.; Oku, H.
Neutralization of hemorrhagic snake venom metalloproteinase HR1a from Protobothrops flavoviridis by human monoclonal antibody
Toxicon
51
345-352
2008
Protobothrops flavoviridis
brenda
Morine, N.; Matsuda, S.; Terada, K.; Iwasaki, H.; Oku, H.
The occurrence of HR1b in the venom of the snake Okinawa habu (Protobothrops flavoviridis)
Biosci. Biotechnol. Biochem.
72
591-594
2008
Protobothrops flavoviridis
brenda