Calo, Sanuele published the artcileConstrained dansyl derivatives reveal bacterial specificity of highly conserved thymidylate synthases, Application In Synthesis of 142335-42-0, the publication is ChemBioChem (2008), 9(5), 779-790, database is CAplus and MEDLINE.
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 for use in DNA synthesis. The present study focused on Lactobacillus casei TS (LcTS) and Escherichia coli TS (EcTS), which exhibit 50% sequence identity and strong folding similarity. The authors have successfully designed and validated a chem. model in which linear, but not constrained, dansyl derivatives specifically complement the LcTS active site. Conversely, chem. constrained dansyl derivatives showed up to 1000-fold improved affinity for EcTS relative to the inhibitory activity of linear derivatives This study demonstrates that the accurate design of small ligands can uncover functional features of highly conserved enzymes.
ChemBioChem published new progress about 142335-42-0. 142335-42-0 belongs to tetrahydroisoquinoline, auxiliary class Tetrahydroisoquinoline,Chiral,Carboxylic acid,Amide,Alcohol, name is (S)-2-(tert-Butoxycarbonyl)-7-hydroxy-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, and the molecular formula is C15H19NO5, Application In Synthesis of 142335-42-0.
Referemce:
https://en.wikipedia.org/wiki/Tetrahydroisoquinoline,
1,2,3,4-Tetrahydroisoquinoline | C9H11N – PubChem