Chemical and enzymatic routes to dihydroxyacetone phosphate


DOI: 10.1007/s00253-007-0882-3

Cite this article as:
Schümperli, M., Pellaux, R. & Panke, S. Appl Microbiol Biotechnol (2007) 75: 33. doi:10.1007/s00253-007-0882-3


Stereoselective carbon–carbon bond formation with aldolases has become an indispensable tool in preparative synthetic chemistry. In particular, the dihydroxyacetone phosphate (DHAP)-dependent aldolases are attractive because four different types are available that allow access to a complete set of diastereomers of vicinal diols from achiral aldehyde acceptors and the DHAP donor substrate. While the substrate specificity for the acceptor is rather relaxed, these enzymes show only very limited tolerance for substituting the donor. Therefore, access to DHAP is instrumental for the preparative exploitation of these enzymes, and several routes for its synthesis have become available. DHAP is unstable, so chemical synthetic routes have concentrated on producing a storable precursor that can easily be converted to DHAP immediately before its use. Enzymatic routes have concentrated on integrating the DHAP formation with upstream or downstream catalytic steps, leading to multi-enzyme arrangements with up to seven enzymes operating simultaneously. While the various chemical routes suffer from either low yields, complicated work-up, or toxic reagents or catalysts, the enzymatic routes suffer from complex product mixtures and the need to assemble multiple enzymes into one reaction scheme. Both types of routes will require further improvement to serve as a basis for a scalable route to DHAP.


Dihyroxyacetone phosphate Aldolases Multi-step reactions 

Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • Michael Schümperli
    • 1
  • René Pellaux
    • 1
  • Sven Panke
    • 1
  1. 1.Bioprocess LaboratoryETH ZurichZurichSwitzerland

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