EC Number   |
Application |
Reference |
|---|
    2.6.1.18 | biotechnology |
an alternative deracemization method for the efficient production of L-homoalanine using D-amino acid oxidase (vide infra) and omega-TA is proposed |
723317 |
| 2.6.1.18 | biotechnology |
recombinant Escherichia coli cells containing overexpressed omega-TA activity are immobilized by entrapment in LentiKats and the effect of permeabilization on free cells and their immobilized counterparts is analyzed. Cells are applied in the synthesis of the aromatic amines 3-amino-1-phenylbutane and 1-phenylethylamine. The best results are obtained with CTAB 0.1% for permeabilization which results in an increase in reaction rate by 40% compared to the whole cells. The synthesis of 1-phenylethylamine is carried out using isopropyl amine and L-alanine as amino donors. Using whole cell biocatalysis, the reaction with isopropyl amine is one order of magnitude faster than with L-alanine |
721915 |
| 2.6.1.18 | more |
the enzyme can be utilized as a catalyst for kinetic resolution of beta-amino acids and amines |
-, 657597 |
| 2.6.1.18 | synthesis |
a prominent example for beta-amino acids in pharmaceuticals is beta-phenylalanine, present in the natural substance paclitaxel (Taxol), which is a prominent anti-cancer agent. Method development for production of chiral beta-phenylalanine ethyl ester, which can be chemically or enzymatically hydrolyzed to (R)- or (S)-phenylalanine. Asymmetric synthesis of the beta-phenylalanine ethyl ester an upscaling, overview |
759802 |
| 2.6.1.18 | synthesis |
enzymatic synthesis of enantiomerically pure (R)-1-phenylethanol and (R)-alpha-methylbenzylamine from racemic alpha-methylbenzylamine in a coupled assay using the omega-transaminase, alcohol dehydrogenase, and glucose dehydrogenase |
-, 658326 |
| 2.6.1.18 | synthesis |
enzymatic synthesis of enantiomerically pure D-beta-amino-n-butyric acid from racemic beta-amino-n-butyric acid |
-, 657597 |
| 2.6.1.18 | synthesis |
optically pure valinol (ee >99%) is prepared employing different omega-transaminases from the corresponding prochiral hydroxy ketone. By the choice of the enzyme the (R)- as well as the (S)-enantiomer are accessible |
737842 |
| 2.6.1.18 | synthesis |
the metabolic removal of pyruvate can be exploited to shift the unfavorable equilibrium of the omega-transaminase-catalyzed amination of ketones using alanine as an amino donor. Vigorous aeration should lead to substantial loss of a volatile ketone substrate without a condenser incorporated into a reactor set-up. A reactor design to support aerobic conditions without undesirable loss of a ketone substrate should be considered |
737864 |
