Reaction Details |
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Target | Serine protease 1 |
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Ligand | BDBM50286441 |
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Substrate/Competitor | n/a |
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Meas. Tech. | Tyrpsin Amidolytic Assay |
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pH | 7.5±n/a |
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Ki | 8.0±0.7 nM |
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Comments | extracted |
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Citation | Markowska, A; Bruzgo, M; Surazynski, A; Midura-Nowaczek, K Tripeptides with non-code amino acids as potential serine proteases inhibitors. J Enzyme Inhib Med Chem28:639-43 (2013) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Serine protease 1 |
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Name: | Serine protease 1 |
Synonyms: | Alpha-trypsin chain 1 | Alpha-trypsin chain 2 | Beta-trypsin | Cationic trypsinogen | PRSS1 | Serine protease 1 | TRP1 | TRY1 | TRY1_HUMAN | TRYP1 | Thrombin & trypsin | Trypsin | Trypsin I | Trypsin-1 |
Type: | Enzyme |
Mol. Mass.: | 26557.80 |
Organism: | Homo sapiens (Human) |
Description: | P07477 |
Residue: | 247 |
Sequence: | MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVS
AGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVIN
ARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKIT
SNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIK
NTIAANS
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BDBM50286441 |
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n/a |
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Name | BDBM50286441 |
Synonyms: | (S)-2-((S)-2-Acetylamino-4-(S)-methyl-pentanoylamino)-4-methyl-pentanoic acid (1-formyl-4-guanidino-butyl)-amide | (S)-2-Acetylamino-4-methyl-pentanoic acid [(R)-1-((S)-1-formyl-4-guanidino-butylcarbamoyl)-3-methyl-butyl]-amide | (S)-2-Acetylamino-4-methyl-pentanoic acid [(S)-1-((S)-1-formyl-4-guanidino-butylcarbamoyl)-3-methyl-butyl]-amide | (S)-2-[(S)-2-((S)-2-Acetylamino-4-methyl-pentanoylamino)-4-methyl-pentanoylamino]-5-guanidino-pentanoic acid | (S)-2-acetylamino-4-methyl-pentanoic acid [(S)-2-(1-formyl-4-guanidino-butylamino)-4-methyl-pentanoyl]-amide | 2-Acetylamino-4-methyl-pentanoic acid [1-(1-formyl-4-guanidino-butylcarbamoyl)-3-methyl-butyl]-amide | Ac-LLR-CHO | Ac-Leu-Leu-Arg-H | CHEMBL129157 |
Type | Small organic molecule |
Emp. Form. | C20H38N6O5 |
Mol. Mass. | 442.5529 |
SMILES | CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O |
Structure |
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