Abood, Amira;Al-Fahad, Ahmed;Scott, Alan;Hosny, Alaa El-Dein M. S.;Hashem, Amal M.;Fattah, Azza M. A.;Race, Paul R.;Simpson, Thomas J.;Cox, Russell J. published 《Kinetic characterisation of the FAD dependent monooxygenase TropB and investigation of its biotransformation potential》 in 2015. The article was appeared in 《RSC Advances》. They have made some progress in their research.Computed Properties of C10H12O4 The article mentions the following:
Achieving regio-specific hydroxylation of aromatic compounds remains a major challenge in synthetic chem. By contrast, this transformation is readily accomplished in nature through the action of FAD-dependent monooxygenase enzymes. Here, the authors report the kinetic characterization of one such enzyme, TropB, from the stipitatic acid biosynthetic pathway. Analogs of the TropB natural substrate, 3-methyl-orcinaldehyde, were synthesized and used to examine the substrate selectivity of this enzyme. TropB displays broad substrate tolerance, for instance accepting single-ring aromatic substrates containing a range of C-1 substituents with varying electronic and steric properties. These include nitro, nitrosyl, alkyl, and aryl keto groups. Bicyclic substrates, however, were rejected by TropB. Addnl., C-5 substituents on single-ring aromatic substrates were not tolerated whereas the presence of a 6-Me group is important for substrate binding. Docking studies were employed to study and understand the broad substrate selectivity of TropB and identifies the key structural elements of its substrates. The authors′ work showed that TropB is an attractive target for biocatalyst engineering and industrial aromatic hydroxylation. To complete the study, the researchers used Methyl 2,4-dihydroxy-3,6-dimethylbenzoate (cas: 4707-47-5) .
Methyl 2,4-dihydroxy-3,6-dimethylbenzoate(4707-47-5) is used in biological study as role of androgens in inducing distinct response of epithelial-mesenchymal transition factors in human prostate cancer cells.Computed Properties of C10H12O4
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