Bioorganic & Medicinal Chemistry Letters 2008-11-15

Synthesis of beta-hydroxy-alpha-amino acids with a reengineered alanine racemase.

Kateryna Fesko, Lars Giger, Donald Hilvert

文献索引：Bioorg. Med. Chem. Lett. 18 , 5987-5990, (2008)

全文：HTML全文

摘要

The Y265A mutant of alanine racemase (alrY265A) was evaluated as a catalyst for the synthesis of beta-hydroxy-alpha-amino acids. It promotes the PLP-dependent aldol condensation of glycine with a range of aromatic aldehydes. The desired products were obtained with complete stereocontrol at C(alpha) (ee>99%, D) and moderate to high selectivity at C(beta) (up to 97% de). The designed enzyme is thus similar to natural d-threonine aldolases in its substrate specificity and stereoselectivity. Moreover, its ability to utilize alanine as an alternative donor suggests an expanded scope of potential utility for the production of biologically active compounds.