type	Journal Article
authors	Osipenkov N, Kulik A, Mast YJ
title	Characterization of the phenylglycine aminotransferase PglE from Streptomyces pristinaespiralis
journal	J Biotechnol
Activity	pgat
Family	pgat
sel	selected
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