D2375
N,O-Didansyl-L-tyrosine cyclohexylammonium salt
≥95% (TLC)
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关于此项目
经验公式（希尔记法）:
C33H33N3O7S2 · C6H13N
化学文摘社编号:
分子量:
746.94
UNSPSC Code:
12352200
PubChem Substance ID:
MDL number:
InChI
1S/C33H33N3O7S2.C6H13N/c1-35(2)29-13-5-11-26-24(29)9-7-15-31(26)44(39,40)34-28(33(37)38)21-22-17-19-23(20-18-22)43-45(41,42)32-16-8-10-25-27(32)12-6-14-30(25)36(3)4;7-6-4-2-1-3-5-6/h5-20,28,34H,21H2,1-4H3,(H,37,38);6H,1-5,7H2/t28-;/m0./s1
SMILES string
NC1CCCCC1.CN(C)c2cccc3c(cccc23)S(=O)(=O)N[C@@H](Cc4ccc(OS(=O)(=O)c5cccc6c(cccc56)N(C)C)cc4)C(O)=O
InChI key
MVXVRKZUVTWXRD-JCOPYZAKSA-N
assay
≥95% (TLC)
form
solid
technique(s)
ligand binding assay: suitable
storage temp.
−20°C
Biochem/physiol Actions
N,O-Didansyl-L-tyrosine (DDT), a potent inhibitor of bacterial thymidylate synthases, is used as a starting lead for development of novel non-substrate-like inhibitors of bacterial thymidylate synthase.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
T A Fritz et al.
Chemistry & biology, 8(10), 981-995 (2001-10-09)
Protein plasticity in response to ligand binding abrogates the notion of a rigid receptor site. Thus, computational docking alone misses important prospective drug design leads. Bacterial-specific inhibitors of an essential enzyme, thymidylate synthase (TS), were developed using a combination of
Sanuele Calò et al.
Chembiochem : a European journal of chemical biology, 9(5), 779-790 (2008-03-18)
The elucidation of the structural/functional specificities of highly conserved enzymes remains a challenging area of investigation, and enzymes involved in cellular replication are important targets for functional studies and drug discovery. Thymidylate synthase (TS, ThyA) governs the synthesis of thymidylate
Donatella Tondi et al.
Journal of medicinal chemistry, 48(4), 913-916 (2005-02-18)
N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS
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