| Reaction Details |
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 | Report a problem with these data |
| Target | Dipeptidyl carboxypeptidase |
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| Ligand | BDBM50010477 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1353482 (CHEMBL3269465) |
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| IC50 | 150000±n/a nM |
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| Citation |  Kramer, GJ; Mohd, A; Schwager, SL; Masuyer, G; Acharya, KR; Sturrock, ED; Bachmann, BO Interkingdom pharmacology of Angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes. ACS Med Chem Lett5:346-51 (2014) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Dipeptidyl carboxypeptidase |
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| Name: | Dipeptidyl carboxypeptidase |
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| Synonyms: | DCP_ECOLI | Dipeptidyl carboxypeptidase | JW1531 | Peptidyl-dipeptidase dcp | dcp |
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| Type: | PROTEIN |
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| Mol. Mass.: | 77504.73 |
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| Organism: | Escherichia coli (strain K12) |
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| Description: | ChEMBL_108355 |
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| Residue: | 681 |
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| Sequence: | MTTMNPFLVQSTLPYLAPHFDQIANHHYRPAFDEGMQQKRAEIAAIALNPQMPDFNNTIL
ALEQSGELLTRVTSVFFAMTAAHTNDELQRLDEQFSAELAELANDIYLNGELFARVDAVW
QRRESLGLDSESIRLVEVIHQRFVLAGAKLAQADKAKLKVLNTEAATLTSQFNQRLLAAN
KSGGLVVNDIAQLAGMSEQEIALAAEAAREKGLDNKWLIPLLNTTQQPALAEMRDRATRE
KLFIAGWTRAEKNDANDTRAIIQRLVEIRAQQATLLGFPHYAAWKIADQMAKTPEAALNF
MREIVPAARQRASDELASIQAVIDKQQGGFSAQPWDWAFYAEQVRREKFDLDEAQLKPYF
ELNTVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDHNGVGLALFYGDFFARDS
KSGGAWMGNFVEQSTLNKTHPVIYNVCNYQKPAAGEPALLLWDDVITLFHEFGHTLHGLF
ARQRYATLSGTNTPRDFVEFPSQINEHWATHPQVFARYARHYQSGAAMPDELQQKMRNAS
LFNKGYEMSELLSAALLDMRWHCLEENEAMQDVDDFELRALVAENMDLPAIPPRYRSSYF
AHIFGGGYAAGYYAYLWTQMLADDGYQWFVEQGGLTRENGLRFREAILSRGNSEDLERLY
RQWRGKAPKIMPMLQHRGLNI
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| BDBM50010477 |
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| n/a |
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| Name | BDBM50010477 |
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| Synonyms: | CHEMBL1233799 |
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| Type | Small organic molecule |
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| Emp. Form. | C25H34N3O8P |
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| Mol. Mass. | 535.5265 |
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| SMILES | CC[C@H](C)[C@H](NC(C)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccc(O)cc1)P(O)(O)=O |r| |
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| Structure | 
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