Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins

Phaseolotoxins (PHTs), which are produced by Pseudomonas, belong to a family of phosphoramidate natural products. Two nonproteinogenic amino acid precursors, N(δ)(N′‐sulfo‐diaminophosphinyl)‐ornithine (PSOrn) and homoarginine (hArg), are involved in biosynthesis of PHTs. Amidinotransferase AmtA cata...

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Autores principales: Li, Mi, Chen, Li, Deng, Zixin, Zhao, Changming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4887976/
https://www.ncbi.nlm.nih.gov/pubmed/27419063
http://dx.doi.org/10.1002/2211-5463.12071
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author Li, Mi
Chen, Li
Deng, Zixin
Zhao, Changming
author_facet Li, Mi
Chen, Li
Deng, Zixin
Zhao, Changming
author_sort Li, Mi
collection PubMed
description Phaseolotoxins (PHTs), which are produced by Pseudomonas, belong to a family of phosphoramidate natural products. Two nonproteinogenic amino acid precursors, N(δ)(N′‐sulfo‐diaminophosphinyl)‐ornithine (PSOrn) and homoarginine (hArg), are involved in biosynthesis of PHTs. Amidinotransferase AmtA catalyses the formation of hArg, with arginine and lysine as substrates. AmtA was overexpressed and purified in an Escherichia coli system. An in vitro enzyme assay showed that it has stricter substrate specificity than certain other amidinotransferases. Site‐directed mutagenesis experiments showed that the mutation AmtA Met243His244 is an alternative while Met246 is essential for the transamidination activity.
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spelling pubmed-48879762016-07-14 Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins Li, Mi Chen, Li Deng, Zixin Zhao, Changming FEBS Open Bio Research Articles Phaseolotoxins (PHTs), which are produced by Pseudomonas, belong to a family of phosphoramidate natural products. Two nonproteinogenic amino acid precursors, N(δ)(N′‐sulfo‐diaminophosphinyl)‐ornithine (PSOrn) and homoarginine (hArg), are involved in biosynthesis of PHTs. Amidinotransferase AmtA catalyses the formation of hArg, with arginine and lysine as substrates. AmtA was overexpressed and purified in an Escherichia coli system. An in vitro enzyme assay showed that it has stricter substrate specificity than certain other amidinotransferases. Site‐directed mutagenesis experiments showed that the mutation AmtA Met243His244 is an alternative while Met246 is essential for the transamidination activity. John Wiley and Sons Inc. 2016-05-16 /pmc/articles/PMC4887976/ /pubmed/27419063 http://dx.doi.org/10.1002/2211-5463.12071 Text en © 2016 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Li, Mi
Chen, Li
Deng, Zixin
Zhao, Changming
Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins
title Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins
title_full Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins
title_fullStr Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins
title_full_unstemmed Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins
title_short Characterization of AmtA, an amidinotransferase involved in the biosynthesis of phaseolotoxins
title_sort characterization of amta, an amidinotransferase involved in the biosynthesis of phaseolotoxins
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4887976/
https://www.ncbi.nlm.nih.gov/pubmed/27419063
http://dx.doi.org/10.1002/2211-5463.12071
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