EC Number |
Application |
Reference |
---|
4.1.2.48 | biotechnology |
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 |
4.1.2.48 | pharmacology |
biotechnological potential for the syntheses of pharmaceutically relevant drug molecules because of the stereospecificity |
747174 |
4.1.2.48 | synthesis |
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 |
4.1.2.48 | synthesis |
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 |
4.1.2.48 | synthesis |
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 |