One-pot, two-step cascade synthesis of naturally rare L-$erythro$ (3S,4S) ketoses by coupling thermostable transaminase and transketolase.

Marion Lorillière (1) , Maxime De Sousa (1) , Felipe Bruna (1) , Egon Heuson (1) , Thierry Gefflaut (1) , Véronique de Berardinis (2) , Thangavelu Saravanan (3) , Dong Yi (3) , Wolf-Dieter Fessner (3) , Franck Charmantray (1) , Laurence Hecquet (1)

1 ICCF - Institut de Chimie de Clermont-Ferrand
2 UMR 8030 - Génomique métabolique
3 Institut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Darmstadt

An efficient simultaneous cascade of two enzymatic steps catalyzed by a thermostable transaminase and transketolase was performed at elevated temperatures allowing the synthesis of naturally rare L-erythro (3S,4S) ketoses. L-ribulose, 5-deoxy-L-ribulose, D-tagatose and L-psicose, which are highly valuable chiral building blocks and display prominent biological properties, were obtained on a preparative scale with excellent stereoselectivities and good yields. A thermostable transketolase from Geobacillus stearothermophilus catalyzed at high temperatures the stereospecific synthesis of L-erythro (3S,4S)-configured ketoses from (2S)-hydroxylated aldehydes and β-hydroxypyruvate in which the latter is generated in an unprecedented manner in situ from natural L-serine and pyruvate using a novel thermostable L-α-transaminase from the thermophilic bacterium Thermosinus carboxydivorans. Overall, this cascade synthesis prevents the thermal decomposition of the labile β-hydroxypyruvate and offers an efficient and environmentally friendly procedure.

Domaines: Chimie

Marion Lorillière, Maxime De Sousa, Felipe Bruna, Egon Heuson, Thierry Gefflaut, et al.. One-pot, two-step cascade synthesis of naturally rare L-$erythro$ (3S,4S) ketoses by coupling thermostable transaminase and transketolase.. Green Chemistry, 2017, 19, pp.425-435. ⟨10.1039/C6GC02015A⟩. ⟨hal-01540859⟩