Microbial aldolases as C-C bonding enzymes--unknown treasures and new developments

Appl Microbiol Biotechnol. 2006 Jul;71(3):253-64. doi: 10.1007/s00253-006-0422-6. Epub 2006 Apr 14.


Aldolases are a specific group of lyases that catalyze the reversible stereoselective addition of a donor compound (nucleophile) onto an acceptor compound (electrophile). Whereas most aldolases are specific for their donor compound in the aldolization reaction, they often tolerate a wide range of aldehydes as acceptor compounds. C-C bonding by aldolases creates stereocenters in the resulting aldol products. This makes aldolases interesting tools for asymmetric syntheses of rare sugars or sugar-derived compounds as iminocyclitols, statins, epothilones, and sialic acids. Besides the well-known fructose 1,6-bisphosphate aldolase, other aldolases of microbial origin have attracted the interest of synthetic bio-organic chemists in recent years. These are either other dihydroxyacetone phosphate aldolases or aldolases depending on pyruvate/phosphoenolpyruvate, glycine, or acetaldehyde as donor substrate. Recently, an aldolase that accepts dihydroxyacetone or hydroxyacetone as a donor was described. A further enlargement of the arsenal of available chemoenzymatic tools can be achieved through screening for novel aldolase activities and directed evolution of existing aldolases to alter their substrate- or stereospecifities. We give an update of work on aldolases, with an emphasis on microbial aldolases.

Publication types

  • Review

MeSH terms

  • Aldehyde-Lyases / classification
  • Aldehyde-Lyases / metabolism*
  • Bacteria / enzymology*
  • Biotechnology / methods
  • Carbon / chemistry*
  • Carbon / metabolism*
  • Dihydroxyacetone / metabolism
  • Stereoisomerism
  • Substrate Specificity


  • Carbon
  • Aldehyde-Lyases
  • Dihydroxyacetone