کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1364599 | 981540 | 2008 | 4 صفحه PDF | دانلود رایگان |
The Y265A mutant of alanine racemase (alrY265A) was evaluated as a catalyst for the synthesis of β-hydroxy-α-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 Cα (ee > 99%, D) and moderate to high selectivity at Cβ (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.
The Y265A mutant of alanine racemase catalyzes the stereoselective condensation of glycine or alanine with a range of aromatic aldehydes.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 18, Issue 22, 15 November 2008, Pages 5987–5990