Biocatalysis provides a highly efficient platform for the synthesis of nonstandard beta-hydroxy-alpha-amino acids, which are important molecules for organic synthesis, medicinal chemistry, chemical biology, and biochemistry. Biocatalytic approaches utilize aldolase or transaldolase enzymes to catalyze an aldol reaction of a pyridoxal phosphate glycyl quinonoid nucleophile and an aldehyde electrophile. This results in nonstandard beta-hydroxy-alpha-amino acids with a side chain that varies depending on the aldehyde substrate used in the reaction. Some disadvantages of aldehyde as substrates for enzyme-catalyzed reactions include their propensity to engage with nucleophilic residues and participate in unwanted side reactions. To overcome these limitations, we studied the efficiency of several aldehyde surrogates in an enzyme-catalyzed trans aldol reaction of L-threonine. This presentation will describe the synthesis of several aldehyde surrogates and their subsequent conversion into nonstandard beta-hydroxy-alpha-amino acids under biocatalytic conditions.

Efficiency of aldehyde surrogates in the synthesis of nonstandard amino acids under biocatalytic conditions that utilize a transaldolase enzyme

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