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Chemical Structure| 2460-33-5 Chemical Structure| 2460-33-5

Structure of 2460-33-5

Chemical Structure| 2460-33-5

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Product Details of [ 2460-33-5 ]

CAS No. :2460-33-5
Formula : C11H12O5
M.W : 224.21
SMILES Code : O=C(CC1=CC=C(OC)C(OC)=C1)C(O)=O
MDL No. :MFCD01090943

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Application In Synthesis of [ 2460-33-5 ]

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

  • Downstream synthetic route of [ 2460-33-5 ]

[ 2460-33-5 ] Synthesis Path-Downstream   1~1

  • 1
  • [ 2460-33-5 ]
  • [ 32161-30-1 ]
YieldReaction ConditionsOperation in experiment
89.6% With L-Aspartic acid; pyridoxal 5'-phosphate; sodium hydroxide; In water; for 12.0h;pH 8;Inert atmosphere; Microbiological reaction; Industrial scale; General procedure: According to our protocols [24-27], the fermentation was operated in a 7 L scale. At the end of the fermentation process, fermentation broth was centrifuged to obtain wet cells. The wet cells were lyophilized and collected after fermentation with a weight of 58.8 ± 1.4 g, which were then mixed with substrates under the optimum reaction conditions for bioconversion in a 20 L reactor. The bioconversion of methoxy substituted phenylalanine was generally operated as follows: L-Asparate (1317.7 g, 9.9 mol) and phenylpyruvate substrates powder (3 mol) were dissolved in water to make 15 L solution. The pH of the resulting solution was adjusted with 2M sodium hydroxide to 8, and then 0.001215 mol PLP, 300 mL Triton X-100 (10%, v/v), and the engineered 170a AspAT cells (75 g) were added successively. The remaining phenylpyruvate substrates were separately added (3 mol, 1.5 mol and 1.5 mol) at intervals of 1 h. The reaction mixture was stirred under N2 at 220 rpm for 12 h after the complete addition. L-DM-Phe precipitated with progressing bioconversion reaction, and the post-treatment of L-DM-Phe was similar to that of L-tyrosine [24,25]. The reaction mixture was centrifuged, and the collected L-DMPhe was purified according to the difference of solubility at the different pH (see supporting information). The spectral characterization of L-DMPhe was shown as follows: [alpha]D25 = -4.3 (lit11=-4.4, c=1, 4M hydrochloric acid), 1H NMR (D2O) (Bruker DRX600, Germany) delta: 6.88 (d, 1H, J=8.2 Hz), 6.81 (s, 1H), 6.75 (dd, 1H, J=1.2 Hz, 8.2 Hz), 3.76 (s, 3H), 3.74 (s, 3H), 3.38 (dd, 1H, J=5.9 Hz, 6.8 Hz), 2.84 (dd, 1H, J=5.5 Hz, 13.6 Hz), 2.70 (dd, 1H, J=7.2 Hz, 13.6 Hz). 13C NMR (D2O, Bruker DRX600, Germany) delta: 182.4, 147.8, 146.7, 131.3, 122.0, 112.9, 111.8, 57.3, 55.7, 55.6, 40.3 (Fig. S1-2). Based on the similar operation, the other methoxy substituted phenylalanines were obtained, and their structures were confirmed by 1H NMR and 13C NMR as shown in Supporting information (Fig. S3-10).
 

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