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(benzyloxycarbonyl-Phe-Arg)2-R110 + H2O
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rhodamine-labeled substrate
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2-aminobenzoic acid-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ala + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Ala-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ala-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Arg-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Asn-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Asn-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Gln-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gln-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Glu-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Glu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Gly-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-His-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-His-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Ile-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Ile-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Leu-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Leu-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Arg-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Arg-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Asn-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asn-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Asp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Asp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Gln-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gln-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Glu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Glu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Gly-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Gly-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-His-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-His-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Ile-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ile-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Ala-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
?
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?
2-aminobenzoyl-Lys-Leu-Arg-Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Arg-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Asn-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gln-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Glu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Gly-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + His-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ile-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Leu-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Phe-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Pro-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ala-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Arg-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Asn-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gln-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Glu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Gly-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-His-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ile-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Leu-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Phe-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Pro-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Ser-Val-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Arg-Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Arg + Val-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Asn-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asn + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Asp-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Asp + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Gln-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gln + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Glu-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Glu + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Gly-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Gly + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-His-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-His + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Ile-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ile + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Lys-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Lys + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Met-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Met + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Lys-Leu-Phe-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Phe + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Pro-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Pro + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Ser-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Ser + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Lys-Leu-Thr-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Thr + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Leu-Val-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Leu-Val + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys-Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Lys-epsilon-amino-caproic acid-Glu-Leu-Lys + Leu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Met-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Met-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Phe-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Phe-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Pro-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Pro-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Ser-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Ser-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Thr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Thr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Trp-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Trp-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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2-aminobenzoyl-Lys-Tyr-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Tyr-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Lys-Val-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Lys-Val-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Trp-NH2 + H2O
2-aminobenzoyl-Met-Ile-Ser-Leu-Met-Lys + Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + 2-aminobenzoyl-Met-Ile-Ser-Leu-Met + Lys-Arg-Pro-Pro-Gly-Trp-Ser-Pro-Phe-Arg + Ser-Ser-Arg-Ile-Trp-NH2
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?
2-aminobenzoyl-Phe-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Phe-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
2-aminobenzoyl-Val-Leu-Arg-Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Val-Leu-Arg + Ser-Ser-Lys-Gln-N-(2,4-dinitrophenyl)ethylenediamine
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?
3-carboxypropionyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
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48 kDa intermediate of cathepsin D + H2O
34 kDa mature cathepsin D + ?
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Abz-3-biphenyl-L-Ala-Arg-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ala-3-nitrotyrosineamide
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?
Abz-3-biphenyl-L-Ala-Arg-Ala-Gln-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Gln-3-nitrotyrosineamide
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?
Abz-3-biphenyl-L-Ala-Arg-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
Abz-3-biphenyl-L-Ala-Arg + L-Ala-Ser-3-nitrotyrosineamide
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Abz-PR-acetyl-K-QLATKAARKSAK-Dnp + H2O
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Abz-PRKQLAT-acetyl-K-AARKSAK-Dnp + H2O
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Abz-PRKQLATKAAR-dimethyl-K-SAK-Dnp + H2O
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?
Abz-PRKQLATKAARKSAK-Dnp + H2O
?
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?
acetyl-AGPRNAA-N-methyl amide + H2O
acetyl-AGPR + NAA-N-methyl amide
docking study
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actomyosin + H2O
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endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi
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alpha-casein + H2O
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?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
BAM-22P + H2O
(Met)enkephalin + ?
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?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
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?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
benzoyl-Phe-Ala-Arg-4-methoxy-2-naphtylamide + H2O
benzoyl-Phe-Ala-Arg + 4-methoxy-2-naphthylamine
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
28.61% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-citrulline-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-L-citrulline 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Leu-L-Glu-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Leu-L-Glu + 7-amino-4-methylcoumarin
76.66% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
cathepsin L specific synthetic substrate
-
-
?
benzyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methyl-coumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Lys-Arg + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Lys-Gln-Lys-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
preferred substrate
-
-
?
benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Phe-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methoxy-beta-naphthylamide + H2O
benzyloxycarbonyl-Phe-Arg + 4-methoxy-beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Bovine serum albumin + H2O
?
cathepsin D + H2O
?
-
-
-
-
?
Cbz-Phe-Arg-7-amido-4-methylcoumarin + H2O
Cbz-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CCAAT-displacement protein/cut homeobox protein + H2O
p90 isoform of CCAAT-displacement protein/cut homeobox protein + p110 isoform of CCAAT-displacement protein/cut homeobox protein + ?
-
-
-
-
?
CCALNNGGGALVPRGSGTAK-(5-carboxyfluorescein)-NH2 + H2O
?
-
-
-
-
?
Cholecystokinin + H2O
?
-
-
-
-
?
chromogranin A + H2O
catestatin
-
-
-
-
?
chromogranin A + H2O
catestatin fragments + ?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen XVIII + H2O
endostatin + ?
-
-
-
-
?
CUX1 transcription factor + H2O
?
-
-
-
-
?
CV-(L-Phe-Arg)2 + H2O
?
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
D-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
Disrupted in renal carcinoma 2 + H2O
?
-
the substrate is proteolytically processed into a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment, respectively. The cleavage site is between amino acid residues 214 and 261
-
-
?
dynamin + H2O
?
CatL is highly reactive toward recombinant dynamin at pH 5.0 and 6.0
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
epidermal growth factor receptor + H2O
?
-
-
-
-
?
FabA antibody + H2O
?
model protein, determination of fragments compared to the recombinant murine enzyme
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
GABARAP-II protein + H2O
?
-
-
-
-
?
gamma-globulin + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
glycogen phosphorylase + H2O
?
-
-
-
-
?
H2N-Abz-DLVGDVRLAGV-3-nitroYA-CONH2 + H2O
?
-
-
-
-
?
histone + H2O
?
-
-
-
-
?
histone H1 + H2O
?
-
-
-
-
?
immunoglobulin G + H2O
?
-
-
-
?
insulin + H2O
?
-
-
-
-
?
insulin receptor + H2O
?
-
-
-
-
?
insulin-like growth factor-1 receptor + H2O
?
-
-
-
-
?
interleukin-8 precursor + H2O
?
-
enzyme plays an important role in IL-8 processing in inflammatory sites
-
?
kininogen + H2O
kinin + ?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
28.66% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
L-arginine 7-amido-4-methylcoumarin + H2O
?
-
very poor substrate
-
-
?
L-lactate dehydrogenase + H2O
?
-
-
-
-
?
L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
L-Val-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
L-Val-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
LC3-II protein + H2O
?
-
-
-
-
?
Leu-Trp-Met-Arg-Phe-Ala + H2O
Leu-Trp-Met + Arg-Phe-Ala
-
-
-
?
Leu-Tyr-7-amido-4-methylcoumarin + H2O
Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
methionine enkephalin-Arg-Arg + H2O
?
-
-
-
-
?
methionine enkephalin-Arg-Phe + H2O
?
-
-
-
-
?
myosin heavy chain + H2O
?
N-acetyl-Phe-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Phe-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-2-(4-methoxynaphthylamide) + H2O
N-benzyloxycarbonyl-Phe-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-carbobenzoxy-L-arginine-L-arginine 7-amido-4-methylcoumarin + H2O
?
-
7% of the activity with N-carbobenzoxy-L-phenylalanine-L-arginine 7-amido-4-methylcoumarin
-
-
?
N-carbobenzoxy-L-phenylalanine-L-arginine 7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N2-benzoyl-L-argininamide + H2O
NH3 + N2-benzoyl-L-arginine
-
-
-
?
Nalpha-benzoyl-L-Arg 2-naphthylamide + H2O
Nalpha-benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
Nalpha-benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Nipah virus fusion protein + H2O
?
phosphorylase a + H2O
?
-
-
-
-
?
precursor form 77IL-8 of interleukin-8 + H2O
precursor form 72IL-8 of interleukin-8 + ?
-
cleavage between Arg5 and Ser6
-
?
pro-dipeptidyl peptidase I
?
pro-dynorphin + H2O
?
-
-
-
-
?
pro-enkephalin + H2O
enkephalin + ?
-
-
-
-
?
pro-neuropeptide Y + H2O
neuropeptide Y + ?
cathepsin L cleaves pro-neuropeptide Y (1-70) to generate neuropeptide Y-Gly (1-38) and the COOH-terminal peptide fragment (39-70)
-
-
?
Pro-opiomelanocortin + H2O
?
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
?
-
-
-
-
?
procathepsin L + H2O
cathepsin L + ?
autoactivation
-
-
?
proheparanase + H2O
active form of heparanase + ?
secretory leukocyte protease inhibitor + H2O
?
-
incubation of recombinant secretory leukocyte protease inhibitor with cathepsin L leads to complete loss of activity while encapsulation of recombinant secretory leukocyte protease inhibitor in 1,2-dioleoyl-sn-glycero-3-[phospho-L-serine]-cholesterol liposomes retains 92.6% of its activity after challenge with cathepsin L
-
-
?
soluble type I collagen + H2O
?
kinetics of collagen binding to cathepsin L, overview. The enzyme cleaves after residue Gln24, the recognition sequence is Gly-Phe-Gln-/-Gly-Pro-Pro (corresponding to positions P3 to P3')
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Tyr-Met-2-naphthylamide + H2O
?
-
-
-
-
?
surimi protein + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Arg-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Val-Pro-Arg-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
1% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
thyroglobulin type-1 domain + H2O
?
-
the thyroglobulin type-1 domain is a protein module that occurs in a variety of secreted and membrane proteins and is recognised as a potent inhibitor of cysteine proteases. Nevertheless, at high enzyme and inhibitor concentrations in the mircomolar range cathepsin L degrades thyroglobulin type-1 domain
-
-
?
topoisomerase-IIalpha + H2O
?
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
trypsinogen + H2O
trypsin + ?
-
cathepsin L inactivates human trypsinogen, CTSL-induced cleavage of trypsinogen occurs 3 amino acids toward the C-terminus from the cathepsin B activation site and results in a truncated, inactive form of trypsin and an elongated propeptide (trypsinogen activation peptide)
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr-Gly + Gly-Phe-Leu
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg + H2O
Tyr-Gly + Gly-Phe-Leu-Arg
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Leu-Arg-Arg
-
-
-
?
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile + H2O
Tyr-Gly + Gly-Phe-Leu-Arg-Arg-Ile
-
-
-
?
Tyr-Gly-Gly-Phe-Met + H2O
Tyr-Gly + Gly-Phe-Met
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Met-Arg-Arg
Tyr-Gly-Gly-Phe-Met-Arg-Gly-Leu + H2O
?
-
cleavage sites Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Phe + H2O
?
-
cleavage sites: Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Phe-NH2 + H2O
?
-
cleavage sites Gly-Gly and Met-Arg
-
-
?
Tyr-Gly-Gly-Phe-Met-NH2 + H2O
Tyr-Gly + Gly-Phe-Met-NH2
Z-Phe-Arg-7-amido-4-methyl-coumarin + H2O
?
-
5 microM, pH 6.5, 28°C
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
Z-Val-Val-Arg-AMC + H2O
Z-Val-Val-Arg + 7-amino-4-methylcoumarin
a cathepsin L-specific substrate
-
-
?
Zaire Ebola virus glycoprotein + H2O
?
-
-
three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding
-
?
additional information
?
-
Albumin + H2O
?
-
isoform CatL5 shows weak activity against albumin
-
-
?
Albumin + H2O
?
-
-
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
no activity
-
-
?
Arg-4-methylcoumarin 7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
low activity
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
7% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
no activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
no activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
weak activity
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
9% activity compared to benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Arg-L-Arg + 7-amino-4-methylcoumarin
88.77% activity compared to benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
100% activity
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
preferred substrate
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
substrate for both cathepsin L and cathepsin B
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
most efficient substrate
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
substrate for both cathepsin L and cathepsin B
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
casein + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
substrate for cathepsin L mutant A205L
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
selective cleavage of terminal peptides leads to conversion of beta- and higher components mainly to alpha-chains
-
-
?
Collagen + H2O
?
-
conversion of cross-linked beta-chain dimers into uncross-linked alpha-chain monomers
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Elastin + H2O
?
-
tritiated elastin
-
-
?
Elastin + H2O
?
-
the enzyme shows distinctive preferences in degrading elastins from bovine neck ligament, aorta, and lung
-
-
?
Elastin + H2O
?
-
-
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
recombinant endorepellin is an in vitro substrate. Inhibition of cathepsin L activity in endothelial cells exposed to pro-apoptotic stimuli prevents release of anti-apoptotic C-terminal fragment of endorepellin without modulating the development of apoptosis. Inhibition of caspase-3 activation in endothelial cells concomitantly prevents cathepsin L release, production of anti-apoptotic C-terminal fragment of endorepellin, and the development of paracrine anti-apoptotic activity
-
-
?
endorepellin + H2O
anti-apoptotic C-terminal fragment of endorepellin + ?
-
recombinant endorepellin is an in vitro substrate
-
-
?
fibronectin + H2
?
-
enzyme cleaves fibronectin to produce two bands
-
?
fibronectin + H2
?
-
enzyme cleaves fibronectin to produce two bands
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
cleavage occurs only at pH 5.5
-
-
?
Fibronectin + H2O
?
-
cleavage occurs only at pH 5.5
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
on gelatin-zymography, the purified pro-mature enzyme of cathepsin L is capable of hydrolyzing 0.1% gelatin at pH 7.5
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
low activity
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
histone H3 + H2O
?
-
-
-
?
histone H3 + H2O
?
-
during embryonic stem cell differentiation, histone H3 is proteolytically cleaved at its N-terminus. H3 cleavage may be regulated by covalent modifications present on the histone tail itself
-
-
?
Immunoglobulin + H2O
?
-
-
-
-
?
Immunoglobulin + H2O
?
-
-
-
-
?
Insulin B-chain + H2O
?
-
-
-
?
Insulin B-chain + H2O
?
-
preferential cleavage at: Glu13-Ala14, Leu17-Val18, and Tyr26-Thr27
-
-
?
Insulin B-chain + H2O
?
-
main cleavage sites: Glu13-Ala14 and Tyr26-Thr27, minor cleavage sites: Val2-Asn3, Asn3-Gln4, Cys7-Glu8, Tyr16-Leu17, Leu17-Val18
-
-
?
kininogen + H2O
kinin + ?
-
-
-
-
?
kininogen + H2O
kinin + ?
-
high and low molecular weight kininogen
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
preferred substrate for isoform CatL5
-
-
?
L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
-
-
-
-
?
L-pyroglutamyl-L-Phe-Leu-p-nitroanilide + H2O
L-pyroglutamyl-L-Phe-Leu + p-nitroaniline
-
-
-
-
?
laminin + H2
?
-
-
-
?
Laminin + H2O
?
-
-
-
?
Laminin + H2O
?
-
cleavage occurs only at pH 5.5
-
-
?
Laminin + H2O
?
-
cleavage occurs only at pH 5.5
-
-
?
Laminin + H2O
?
-
-
-
-
?
myosin heavy chain + H2O
?
-
-
-
-
?
myosin heavy chain + H2O
?
-
-
-
-
?
Nipah virus fusion protein + H2O
?
-
proteolytically processed within endosomes by cathepsin L
-
-
?
Nipah virus fusion protein + H2O
?
-
cathepsin L specifically converts Nipah virus fusion protein to a mature and fusogenic form
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
perforin + H2O
?
-
CatL preferentially cleaves a site on full-length recombinant perforin close to its C terminus
-
-
?
pro-dipeptidyl peptidase I
?
-
cleavage at K133
-
?
pro-dipeptidyl peptidase I
?
-
cathepsin L could be an important activator of dipeptidyl peptidase I in vivo
-
?
proheparanase + H2O
active form of heparanase + ?
-
removal of the linker peptide and conversion of proheparanase into its active 8 + 50-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
-
-
?
proheparanase + H2O
active form of heparanase + ?
-
removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L
-
-
?
serum albumin + H2O
?
-
-
-
?
serum albumin + H2O
?
-
-
-
-
?
serum albumin + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Ala-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Asp-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
preferred substrate for isoform CatL1G
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
type 1 collagen + H2O
?
-
isoform Catl1G completely digests collagen type 1
-
-
?
type 1 collagen + H2O
?
-
efficient cleavage of type 1 collagen by isoform CatL5 is limited to the beta-and gamma-chains
-
-
?
Type I collagen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Type I collagen + H2O
?
-
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Met-Arg-Arg
-
-
-
-
?
Tyr-Gly-Gly-Phe-Met-Arg-Arg + H2O
Tyr-Gly + Gly-Phe-Met-Arg-Arg
-
-
-
?
Tyr-Gly-Gly-Phe-Met-NH2 + H2O
Tyr-Gly + Gly-Phe-Met-NH2
-
-
-
-
?
Tyr-Gly-Gly-Phe-Met-NH2 + H2O
Tyr-Gly + Gly-Phe-Met-NH2
-
-
-
?
vitronectin + H2
?
-
-
-
?
vitronectin + H2
?
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
enzyme may involve in invasion of cercaria into fish and development to metacercaria, excystment of metacercaria, and protein digestion of adult
-
-
?
additional information
?
-
no activity with benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin. The recombinant CsCPL-m can degrade bovine serum albumin and gelatin, but can not degrade human hemoglobin and human immunoglobulin G
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additional information
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no activity with benzyloxycarbonyl-L-Arg-L-Arg-7-amido-4-methylcoumarin. The recombinant CsCPL-m can degrade bovine serum albumin and gelatin, but can not degrade human hemoglobin and human immunoglobulin G
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additional information
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proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
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proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
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additional information
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proteolytic activity only under reducing conditions, e.g. in presence of dithiothreitol. No substrate: type IV collagen
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additional information
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owing to its low specificity, cathepsin L is able to cleave a diversity of proteins, it cleaves a variety of recombinant proteins including monoclonal antibodies, antibody fragments, bispecific antibodies, and fusion proteins. Cathepsin L is a low specificity protease. CHO cathepsin L seems to have preferential cleavage sites on mAbs of different subclass as similar fragment profiles exist for three tested mAbs. IgG1 does not interact with cathepsin L
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additional information
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owing to its low specificity, cathepsin L is able to cleave a diversity of proteins, it cleaves a variety of recombinant proteins including monoclonal antibodies, antibody fragments, bispecific antibodies, and fusion proteins. Cathepsin L is a low specificity protease. CHO cathepsin L seems to have preferential cleavage sites on mAbs of different subclass as similar fragment profiles exist for three tested mAbs. IgG1 does not interact with cathepsin L
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additional information
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enzyme activity plays a pivotal role in prolactin-induced spermatogonial apoptosis
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3% with benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin and 1% with both L-Arg-7-amido-4-methylcoumarin and Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin. No activity with Boc-Gln-Arg-Arg-7-amido-4-methylcoumarin and succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin
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additional information
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the cathepsin B and H specific synthetic substrates benzyloxycarbonyl-L-Ala-L-Ala-7-amido-4-trifluoromethylcoumarin and L-Arg-7-amido-4-methylcoumarin do not show any hydrolysis with the partially purified enzyme
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isoform CatL1G can cleave substrates with proline residues at P2, isoform CatL1G is unable to digest albumin or hemoglobin, efficiently at either pH 5.5 or 7.0
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additional information
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isoform CatL1G can cleave substrates with proline residues at P2
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analysis of substrate specificity of FhCL3, strong preference of the cathepsin for Pro and Gly residues at P2 and P3 sites, respectively, of substrates. Residues residues, Q19, G23, G25, W26, G67, W69, Y143, T161, H162 and W184, of FhCL3 largely contribute to the substrate binding. W69, Y143 and T161 have the largest per-residue free energy contributions to the complex formation, interaction analysis, overview
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additional information
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analysis of substrate specificity of FhCL3, strong preference of the cathepsin for Pro and Gly residues at P2 and P3 sites, respectively, of substrates. Residues residues, Q19, G23, G25, W26, G67, W69, Y143, T161, H162 and W184, of FhCL3 largely contribute to the substrate binding. W69, Y143 and T161 have the largest per-residue free energy contributions to the complex formation, interaction analysis, overview
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the enzyme performs autocleavage of its proform
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the enzyme performs autocleavage of its proform
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additional information
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the enzyme performs autocleavage of its proform
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additional information
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no activity with benzyloxycarbonyl-Phe-Ala-4-methylcoumarin 7-amide and with benzyloxycarbonyl-Phe-Met-4-methylcoumarin 7-amide
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additional information
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the enzyme is involved in tissue destruction in arthritis
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additional information
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the enzyme plays a crucial role in the degradation of the invariant chain during maturation of major histocompatibility complex class II molecules and antigen processing
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additional information
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differentiation of human macrophages within the lung is accompanied by synthesis and expression of cathepsin L
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CAT L plays a significant role in numerous important physiological and pathological processes, such as bone resorption, cancer progression and atherosclerosis
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cathepsin L has a pro-survival function within the cell which may be due, at least in part, to its ability to deplete the cells from the proapoptotic molecule caspase-3. The existence of a proteolytic hierarchy between pro-survival and pro-death proteases suggests that changes in cellular proteolytic profiles are likely to have significant consequences not only on its survival but also on the type of death it may undergo in response to a specific stress
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catL is essential for epidermal homeostasis and regular hair follicle morphogenesis and cycling
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contributions of cathepsin L and cathepsin B to autophagic protein degradation of cytoplasmic proteins in HeLa and Huh-7 cells are nearly equal. Cathepsin L does not play a general role in the degradation of proteins in the lumen of autophagosomes, but rather is involved specifically in the degradation of autophagosomal membrane markers
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pituitary gland may utilize the cathepsin L and prohormone convertase pathways for producing propiomelanocortin-derived peptide hormones
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additional information
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the enzyme does not hydrolyze ortho-aminobenzoic acid-VLFEKKVYLQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-KPVSTEQLAQ-N-[2,4-dinitrophenyl]ethylenediamine , Ortho-aminobenzoic acid-KPPVVLLPDQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-LFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, ortho-aminobenzoic acid-VLFEKQ-N-[2,4-dinitrophenyl]ethylenediamine, and ortho-aminobenzoic acid-VLFEKKQ-N-[2,4-dinitrophenyl]ethylenediamine
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additional information
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human cathepsin L shows no proline specificity, but collagenolytic activity. Cathepsin L also is a strong gelatinase. Comparison with cathepsin K, overview
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additional information
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human cathepsin L shows no proline specificity, but collagenolytic activity. Cathepsin L also is a strong gelatinase. Comparison with cathepsin K, overview
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additional information
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the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
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additional information
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the enzyme binds to concanavalin A, but not to Lens culinaris agglutinin, Ricinus communis agglutinin 120 (RCA120), and wheat germ agglutinin
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additional information
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the enzyme performs autocatalytic cleavage
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no activity towards benzyloxycarbonyl-Gly-Gly-L-Arg-7-amido-4-methylcoumarin
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additional information
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p4165aa, a 65 amino acid segment of the p41 splice variant of major histocompatibility complex class II-associated invariant chain, stabilizes cathepsin L in the extracellular environment and induces a local decrease in the concentration of matrix-degrading enzymes during inflammation. Through its interaction with cathepsin L, complex class II-associated invariant chain Ii may control the migratory response of antigen-presenting cells and/or the recruitment of effectors of the inflammatory response
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upon interferon-gamma activation of peritoneal macrophages, enzymatic activityof cathepsin L is specifically inhibited, such that cathepsin S mediates Ii degradation and regulates MHC class II maturation
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cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides
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additional information
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cathepsin L expression levels regulate cell responsiveness to IGF-type I, function for cathepsin L in the control of the tumorigenic/metastatic phenotype
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additional information
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cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
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additional information
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cathepsin L has a prominent role in the production of adrenocorticotropic hormone, beta-endorphin, and alpha-melanocyte stimulating hormone
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additional information
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the enzyme has a preference for hydrophobic amino acids in P2 and P3 residues
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additional information
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the enzyme removes the Ca-sensitivity of ATPase activity of myofibrils
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involved in extracellular food digestion
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the recombinant enzyme is inefficient in hydrolyzing azocasein, fibrinogen, and bovine serum albumin
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additional information
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the enzyme plays a most important role in intralysosomal proteolysis in hepatocytes
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additional information
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plays a crucial role in the pathogenesis of adjuvant arthritis
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basement membrane of larval brains contains two substrate proteins
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the enzyme is suggested to play a crucial role in the degradation of the basement membranes
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no activity with human immunoglobulin
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no activity with human immunoglobulin
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additional information
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enzyme has a role in the progress of the cell cycle during the cleavage divisions of embryonic development. Inhibition of the protease abolishes the chromatin decondensation after mitosis
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additional information
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granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
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additional information
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granular amoebocytes immunopositive for cathepsin L are chemoattracted to the site of injury and phagocyte bacteria
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additional information
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leucine is preferred over phenylalanine in position P2
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