Substrate specificity and stereochemical source of TKasecatalyzed reaction

Through extensive screening of compounds,32-38 42-58 it was revealed that this enzyme accepts a very wide range of substrates. In addition to phosphorylated aldose, which are the native substrate, non-phosphorylated aldose, simple aliphatic, aromatic, heterocyclic and functionalized aldehydes, even with an increased hydropho-bicity, work as substrates. The stereochemical course has been elucidated in Fig. 18. The hydroxyl group on the 2-position of the aldehyde is very important55 and 2-deoxygenated aldehydes were rather weak substrates. The substrates with d-configuration at the 2-position have a stronger affinity to TKase than L-form.

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