504-15-4Relevant articles and documents
Bram,C.
, p. 4069 - 4072 (1967)
COMPOUNDS, COMPOSITIONS, AND METHODS FOR MODULATING SWEET TASTE
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Paragraph 0358; 0360, (2021/09/17)
The present disclosure provides edible compositions comprising a flavor-grade sweet taste modulator or a combination of flavor-grade sweet taste modulators or a flavor-grade bitter taste blocker or a combination of flavor-grade bitter taste blockers of the present disclosure, food products comprising such edible compositions and methods of preparing such food products. The present disclosure also provides methods of reducing the amount of sugar in a food product, methods of reducing the caloric intake in a diet, and methods of enhancing sweet taste or blocking a bitter taste in a food product.
Synthesis of Substituted Anilines from Cyclohexanones Using Pd/C-Ethylene System and Its Application to Indole Synthesis
Maeda, Katsumi,Matsubara, Ryosuke,Hayashi, Masahiko
supporting information, p. 1530 - 1534 (2021/03/08)
The synthesis of anilines and indoles from cyclohexanones using a Pd/C-ethylene system is reported. A simple combination of NH4OAc and K2CO3 under nonaerobic conditions was found to be the most suitable to perform this reaction. Hydrogen transfer between cyclohexanone and ethylene generates the desired products. The reaction tolerates a variety of substitutions on the starting cyclohexanones.
Mechanism and Structure of γ-Resorcylate Decarboxylase
Sheng, Xiang,Patskovsky, Yury,Vladimirova, Anna,Bonanno, Jeffrey B.,Almo, Steven C.,Himo, Fahmi,Raushel, Frank M.
, p. 3167 - 3175 (2018/06/11)
γ-Resorcylate decarboxylase (γ-RSD) has evolved to catalyze the reversible decarboxylation of 2,6-dihydroxybenzoate to resorcinol in a nonoxidative fashion. This enzyme is of significant interest because of its potential for the production of γ-resorcylate and other benzoic acid derivatives under environmentally sustainable conditions. Kinetic constants for the decarboxylation of 2,6-dihydroxybenzoate catalyzed by γ-RSD from Polaromonas sp. JS666 are reported, and the enzyme is shown to be active with 2,3-dihydroxybenzoate, 2,4,6-trihydroxybenzoate, and 2,6-dihydroxy-4-methylbenzoate. The three-dimensional structure of γ-RSD with the inhibitor 2-nitroresorcinol (2-NR) bound in the active site is reported. 2-NR is directly ligated to a Mn2+ bound in the active site, and the nitro substituent of the inhibitor is tilted significantly from the plane of the phenyl ring. The inhibitor exhibits a binding mode different from that of the substrate bound in the previously determined structure of γ-RSD from Rhizobium sp. MTP-10005. On the basis of the crystal structure of the enzyme from Polaromonas sp. JS666, complementary density functional calculations were performed to investigate the reaction mechanism. In the proposed reaction mechanism, γ-RSD binds 2,6-dihydroxybenzoate by direct coordination of the active site manganese ion to the carboxylate anion of the substrate and one of the adjacent phenolic oxygens. The enzyme subsequently catalyzes the transfer of a proton to C1 of γ-resorcylate prior to the actual decarboxylation step. The reaction mechanism proposed previously, based on the structure of γ-RSD from Rhizobium sp. MTP-10005, is shown to be associated with high energies and thus less likely to be correct.
