Functional expression of @entity9108 a-oxidase from XXXX in @entity526 for one-pot synthesis of @entity16443 from DL-lysine.

@entity66 @entity32764 @entity15250 @entity515 @entity9108 @entity376 @entity16443 @entity3881 @entity413 @entity526
UNASSIGNED: @entity16443 is a key component of biologically active molecules and a pharmaceutically important chiral building block. It can be stereoselectively produced from @entity9108 by a two-step bioconversion involving @entity9108 a-oxidase and    (1)-piperideine-2-carboxylae (Pip2C) reductase. In this study, we focused on an @entity9108 a-oxidase from @entity32764 that was originally identified as an @entity66 ( @entity66 ) and applied the enzyme to one-pot fermentation of @entity16443 in @entity526 . A synthetic gene coding for an @entity66 was expressed in @entity526 , and the recombinant enzyme was purified and characterized. The purified enzyme was determined to be a homodimer with a molecular mass of 133.9  kDa. The enzyme essentially exhibited the same substrate specificity as the native enzyme. Optimal temperature and pH for the enzymatic reaction were 70   C  and 7.4, respectively. The enzyme was stable below 60    C and at a pH range of 5.5-7.5 but was markedly inhibited by @entity515 . To establish a one-pot fermentation system for the synthesis of optically pure @entity16443 from DL-lysine, an @entity526 carrying a plasmid encoding @entity66 , Pip2C reductase from @entity15250 , @entity376 racemase from @entity15250 , and @entity413 dehydrogenase from @entity3881 was constructed. The one-pot process produced 45.1  g/L of @entity16443 (87.4  % yield from DL- @entity376 ) after a 46-h reaction with high optical purity (>99.9  % enantiomeric excess).
