모든 사진(1)
About This Item
실험식(Hill 표기법):
C33H33N3O7S2 · C6H13N
CAS Number:
Molecular Weight:
746.94
MDL number:
UNSPSC 코드:
12352200
PubChem Substance ID:
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분석
≥95% (TLC)
양식
solid
기술
ligand binding assay: suitable
저장 온도
−20°C
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
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
InChI key
MVXVRKZUVTWXRD-JCOPYZAKSA-N
생화학적/생리학적 작용
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
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
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
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
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