U. Schorken et Ga. Sprenger, THIAMIN-DEPENDENT ENZYMES AS CATALYSTS IN CHEMOENZYMATIC SYNTHESES, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1385(2), 1998, pp. 229-243
Enzymes are increasingly being used to perform regio- and enantioselec
tive reactions in chemoenzymatic syntheses. To utilize enzymes for unp
hysiological reactions and to yield novel products, a broad substrate
spectrum is desirable. Thiamin diphosphate (ThDP)-dependent enzymes va
ry in their substrate tolerance from rather strict substrate specifici
ty (phosphoketolases, glyoxylate carboligase) to more permissive enzym
es (transketolase, dihydroxyacetone synthase, pyruvate decarboxylase)
and therefore differ in their potential to be used as biocatalysts. We
give an overview of the known substrate spectra of ThDP-dependent enz
ymes and present examples of multi-enzyme or chemoenzymatic approaches
which involve ThDP-dependent enzymes as biocatalysts to obtain pharma
ceutical compounds as ephedrine and glycosidase inhibitors, sex pherom
ones as exo-brevicomin, C-13-labeled metabolites, and other intermedia
tes as 1-deoxyxylulose 5-phosphate, a precursor of vitamins and isopre
noids. (C) 1998 Elsevier Science B.V. All rights reserved.