Reaction Details |
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Target | S-adenosylmethionine decarboxylase proenzyme |
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Ligand | BDBM50366314 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_196570 (CHEMBL800448) |
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IC50 | 178600±n/a nM |
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Citation | Wu, YQ; Lawrence, T; Guo, JQ; Woster, PM -cyano-substituted analogoues of decarboxylated S-adenosylmethionine as enzyme activated, irreversible inhibitors of S-adenosylmethionine decarboxylase Bioorg Med Chem Lett3:2811-2816 (1993) Article |
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More Info.: | Get all data from this article, Assay Method |
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S-adenosylmethionine decarboxylase proenzyme |
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Name: | S-adenosylmethionine decarboxylase proenzyme |
Synonyms: | AMD | AMD1 | DCAM_HUMAN | S-Adenosylmethionine Decarboxylase (AdoMetDC) | S-adenosylmethionine decarboxylase 1 | SAMDC |
Type: | Heterotetramer of two alpha and two beta chains |
Mol. Mass.: | 38337.21 |
Organism: | Homo sapiens (Human) |
Description: | For the production of protein for the hAdoMetDC enzyme assays, the plasmid containing (H)6 tag at the carboxyl end (replacing -QQQQQS) was used. |
Residue: | 334 |
Sequence: | MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKP
SHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEIL
MSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYW
TIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQ
KIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS
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BDBM50366314 |
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n/a |
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Name | BDBM50366314 |
Synonyms: | CHEMBL3392211 | CHEMBL607699 |
Type | Small organic molecule |
Emp. Form. | C14H19N7O3S |
Mol. Mass. | 365.411 |
SMILES | NC(CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12)C#N |r| |
Structure |
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