EC Number   |
Application |
Reference |
|---|
   2.6.1.B21 | synthesis |
amine transaminase (ATA) catalyzing stereoselective amination of prochiral ketones is an attractive alternative to transition metal catalysis |
759050 |
| 2.6.1.B21 | synthesis |
development of a one-pot, trienzymatic cascade comprising an (R)-specific omega-transaminase, an amine dehydrogenase, and a formate dehydrogenase for the economical and ecofriendly synthesis of (R)-chiral amines. Using inexpensive ammonium formate as the sole sacrificial agent, the established cascade system enables efficient omega-transaminase-mediated (R)-amination of various ketones, with high conversions and excellent enantiomeric excess (over 99%), water and CO2 are the only waste products |
-, 759647 |
| 2.6.1.B21 | synthesis |
in another reaction for deracemization using enantiocomplementary transaminases, the oxidative deamination step is carried out by alpha-transaminase such as branched-chain transaminase (EC 2.6.1.42) and D-amino acid transaminase (EC 2.6.1.21). It is notable that substitution of alpha-transaminase with alanine dehydrogenase in the deracemization method for production of D-amino acids using L-alanine dehydrogenase (AlaDH), D-selective omega-transaminase (omega-TA) ARTAmut, and NADH oxidase (NOX) eliminates the need for an expensive 2-oxoacid cosubstrate. Feasibility of the stereoinversion reaction is dependent on enzyme activities of AlaDH and onega-TA for L-amino acids and its keto acids, respectively. ARTAmut substrate specificity allows various oxoacids as substrates |
759007 |
| 2.6.1.B21 | synthesis |
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme |
-, 758848 |
