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B6db references: 29738785

type Journal Article
authors Osipenkov N, Kulik A, Mast YJ
title Characterization of the phenylglycine aminotransferase PglE from Streptomyces pristinaespiralis
journal J Biotechnol
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ui 29738785
year (2018)
volume 278
pages 34-38
keywords Aminotransferase; Antibiotics; Non-proteinogenic amino acid; Phenylglycine; Pristinamycin
abstract L-phenylglycine is a rare non-proteinogenic amino acid, which only occurs in some natural compounds, such as the streptogramin antibiotics pristinamycin I and virginiamycin S or the bicyclic peptide antibiotic dityromycin. Here we report on the biochemical characterization of the aminotransferase PglE that catalyzes the transamination from phenylglyoxylate to L-phenylglycine, which represents the final reaction step during phenylglycine biosynthesis. Enzyme assays with the purified PglE enzyme revealed that L-phenylalanine is used as an amino group donor for the transamination reaction, leading to the formation of phenylpyruvate, which may re-enter phenylglycine biosynthesis as a precursor. Based on these results, we postulate a new model for L-phenylglycine biosynthesis.
last changed 2018/05/14 09:45

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