Safety of Ethyl 2-amino-2-thioxoacetateIn 2002 ,《Anilinoquinazoline Inhibitors of Fructose 1,6-Bisphosphatase Bind at a Novel Allosteric Site: Synthesis, In Vitro Characterization, and X-ray Crystallography》 was published in Journal of Medicinal Chemistry. The article was written by Wright, Stephen W.; Carlo, Anthony A.; Carty, Maynard D.; Danley, Dennis E.; Hageman, David L.; Karam, George A.; Levy, Carolyn B.; Mansour, Mahmoud N.; Mathiowetz, Alan M.; McClure, Lester D.; Nestor, Nestor B.; McPherson, R. Kirk; Pandit, Jayvardhan; Pustilnik, Leslie R.; Schulte, Gayle K.; Soeller, Walter C.; Treadway, Judith L.; Wang, Ing-Kae; Bauer, Paul H.. The article contains the following contents:
Thiazolylphenylaminoquinazolines I (R = H, Me, c-C3H5, EtCH2, Ph, PhCH2, HOCH2, MeOCH2, H2N, MeNH, Me2N, H2NNH, MeO, EtO, HO2C, H2NCO; R1 = H, F; R2 = H, Cl, F; R3 = H, F3C; R4 = H, Br, Cl, F, Me, MeO, Et, EtO; R5 = H, Me, Et, EtCH2, Me2CH, PhCH2, Cl, ClCH2, ClCH2CH2, ClCH2CH2CH2, F3C, MeSO2CH2, MeOCH2, H2NCH2, Me2NCH2, EtNHCH2, 1-pyrrolidinylmethyl, HO2CCH2, 1-imidazolyl, H2NCH2CH2) and other heterocyclyl- and arylphenylaminoquinazolines were prepared and found to act as allosteric inhibitors of fructose-1,6-bisphosphatase (F16BPase); the structure-activity relationship of I to binding at F16BPase and selectivity for F16BPase over the epidermal growth factor receptor tyrosine kinase (EGFR), the original target for I, were evaluated. I have a different SAR as inhibitors of F16Bpase than anilinoquinazolines previously reported. Selective inhibition of F16BPase was attained through the addition of appropriate polar functional groups at the quinazoline 2-position, thus separating the F16BPase inhibitory activity from the epidermal growth factor receptor tyrosine kinase inhibitory activity previously observed with similar structures. Substitution of other heterocycles for the thiazolyl moiety in I gave compounds with variable activities at both F16BPase and at EGFR; the effective inhibitors were selective for EGFR. Alteration of the 6,7-diethoxyquinazoline segment abolished F16BPase inhibition. A symmetry-repeated novel allosteric site present in the homotetrameric form of F16BPase at the interface of its subunits was found to bind I and related anilinoquinazolines. I inhibit F16BPase by binding to a loop comprised of residues 52-72 in the monomer, preventing the necessary participation of these residues in the assembly of the catalytic site. Mutagenesis of glutamine 50 and of glutamine 55 of F16BPase abolish the binding of I and are the key amino acid residues required for inhibitor recognition and binding. The crystal structure of I (R = HOCH2; R1 = R2 = R3 = R4 = R5 = H) bound to porcine kidney F16BPase was determined In the experimental materials used by the author, we found Ethyl 2-amino-2-thioxoacetate(cas: 16982-21-1Safety of Ethyl 2-amino-2-thioxoacetate)
Ethyl 2-amino-2-thioxoacetate(cas: 16982-21-1) belongs to anime. Amines can be classified according to the nature and number of substituents on nitrogen. Aliphatic amines contain only H and alkyl substituents. Aromatic amines have the nitrogen atom connected to an aromatic ring.Important amines include amino acids, biogenic amines, trimethylamine, and aniline. Inorganic derivatives of ammonia are also called amines, such as monochloramine (NClH2).Safety of Ethyl 2-amino-2-thioxoacetate
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