Microbial aldolases as C-C bonding enzymes--unknown treasures and new developments.
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.
Samland
Anne K
AK
Institut für Mikrobiologie, Universität Stuttgart, Germany.
Sprenger
Georg A
GA
D000446:Aldehyde-Lyases / Q000145:classification / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D001709:Biotechnology / Q000379:methods; D002244:Carbon / Q000737:chemistry* / Q000378:metabolism*; D004098:Dihydroxyacetone / Q000378:metabolism; D013237:Stereoisomerism; D013379:Substrate Specificity
D002244:Carbon; D000446:Aldehyde-Lyases; D004098:Dihydroxyacetone