|
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 |
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