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Results 1 - 5 of 5
EC Number Application Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.48biotechnology a continuous bioconversion system for L-threo-3,4-dihydroxyphenylserine production is developed that uses whole-cell biocatalyst of recombinant Escherichia coli expressing L-TA genes cloned from Streptomyces avelmitilis MA-4680. Maximum conversion rates are observed at 2 M glycine, 145 mM 3,4-dihydroxybenzaldehyde, 0.75% Triton-X, 5 g Escherichia coli cells/l, pH 6.5 and 10°C. In the optimized condition, overall productivity is 8 g/l 691447
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.48pharmacology biotechnological potential for the syntheses of pharmaceutically relevant drug molecules because of the stereospecificity 747174
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.48synthesis production of L-threo-3,4-dihydroxyphenylserine. At the optimized conditions, a mixture of L-threo-3,4-dihydroxyphenylserine and L-erythro-3,4-dihydroxyphenylserine is synthesized by diastereoselectivity-enhanced L-threonine aldolase expressed in Escherichia coli in a continuous process for 100 h, yielding an average of 4.0 mg/ml of L-threo-3,4-dihydroxyphenylserine and 60% diastereoselectivity 728649
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.48synthesis synthesis of optically active beta-hydroxy-alpha-amino acids by immobilized Escherichia coli cells expressing the enzyme. The immobilized cells can be continuously used 10 times, yielding an average conversion rate of 60.4% 718557
Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.48synthesis the enzyme may be exploited for bioorganic synthesis of L-3-hydroxyamino acids that are biologically active or constitute building blocks for pharmaceutical molecules 747734
Results 1 - 5 of 5