A photochemically chemically active noncanonical amino acid para-azido-L-phenylalanine widely used in biology was found to be metabolized by Saccharomyces cerevisiae. Contrary to multiple reports, the azide moiety is not reduced to the corresponding amine. The amino acid's concentration was found to decline somewhat with time which was due, at least in part, to modification of the amino acid side chain. The metabolite was found to be photochemically active and further characterization concluded the azide moiety was still intact. This work also goes onto highlight paramount areas of concern with regards to (photo)chemical compatibility, handling, and fidelity in genetically encoding aryl azide amino acids.

中文翻译：

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酵母中芳基叠氮化物非常规氨基酸的新用途†

发现一种广泛用于生物学的具有光化学活性的非规范氨基酸对叠氮基-L-苯丙氨酸可被酿酒酵母代谢。与多个报告相反，叠氮化物部分不还原为相应的胺。发现氨基酸的浓度随时间有所下降，这至少部分是由于氨基酸侧链的修饰。发现该代谢物具有光化学活性，并且进一步表征表明叠氮化物部分仍然完整。这项工作还涉及与遗传相关的芳基叠氮化物氨基酸的（光）化学相容性，处理和保真度方面最重要的重要领域。