Fructose 1,6-Bisphosphate Aldolase fromStaphylococcus carnosus: Overexpression, Structure Prediction, Stereoselectivity, and Application in the Synthesis of Bicyclic Sugars

Abstract

The unusually stable fructose 1,6-bisphosphate aldolase from Staphylococcus carnosus (FruAsca) was overproduced in E. coli. An α=β-barrel structure and highly conserved active site was inferred from sequence analysis in comparison to known class I aldolases. A preparative study with generic aliphatic and hydroxylated aldehydes confirmed a high level of stereoselectivity, and thus a functional equivalence of the Staphylococcus enzyme to the commercial rabbit muscle aldolase for asymmetric synthesis. Despite their high enzyme cross-linking reactivity, glutardialdehyde derivatives could be converted by the Staphylococcus aldolase to give novel bicyclic sugars.