Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana

Abstract The proteinogenic amino acid l-serine is a precursor for various essential biomolecules in all organisms. 3-Phosphoglycerate dehydrogenase (PGDH) is the first committed enzyme of the phosphorylated pathway of l-serine biosynthesis, and is regulated by negative feedback from l-serine in bact...

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Autores principales:	Eiji Okamura, Masami Yokota Hirai
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fe9c7cfe584946ec8fa1d3dc376ccab0
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spelling	oai:doaj.org-article:fe9c7cfe584946ec8fa1d3dc376ccab02021-12-02T15:06:13ZNovel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana10.1038/s41598-017-03807-52045-2322https://doaj.org/article/fe9c7cfe584946ec8fa1d3dc376ccab02017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03807-5https://doaj.org/toc/2045-2322Abstract The proteinogenic amino acid l-serine is a precursor for various essential biomolecules in all organisms. 3-Phosphoglycerate dehydrogenase (PGDH) is the first committed enzyme of the phosphorylated pathway of l-serine biosynthesis, and is regulated by negative feedback from l-serine in bacteria and plants. In the present study, two Arabidopsis PGDH isoforms were inhibited by l-serine but were activated by l-amino acids such as l-homocysteine in vitro. Activation and inhibition by these amino acids was cooperative, suggesting an allosteric mechanism. Moreover, the half maximal effective concentration of l-homocysteine was 2 orders of magnitude lower than that of l-serine, suggesting greater regulatory potency. These are the first data to show that PGDH is activated by various biomolecules and indicate that serine biosynthesis is regulated by multiple pathways.Eiji OkamuraMasami Yokota HiraiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Eiji Okamura Masami Yokota Hirai Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
description	Abstract The proteinogenic amino acid l-serine is a precursor for various essential biomolecules in all organisms. 3-Phosphoglycerate dehydrogenase (PGDH) is the first committed enzyme of the phosphorylated pathway of l-serine biosynthesis, and is regulated by negative feedback from l-serine in bacteria and plants. In the present study, two Arabidopsis PGDH isoforms were inhibited by l-serine but were activated by l-amino acids such as l-homocysteine in vitro. Activation and inhibition by these amino acids was cooperative, suggesting an allosteric mechanism. Moreover, the half maximal effective concentration of l-homocysteine was 2 orders of magnitude lower than that of l-serine, suggesting greater regulatory potency. These are the first data to show that PGDH is activated by various biomolecules and indicate that serine biosynthesis is regulated by multiple pathways.
format	article
author	Eiji Okamura Masami Yokota Hirai
author_facet	Eiji Okamura Masami Yokota Hirai
author_sort	Eiji Okamura
title	Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
title_short	Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
title_full	Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
title_fullStr	Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
title_full_unstemmed	Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
title_sort	novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in arabidopsis thaliana
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/fe9c7cfe584946ec8fa1d3dc376ccab0
work_keys_str_mv	AT eijiokamura novelregulatorymechanismofserinebiosynthesisassociatedwith3phosphoglyceratedehydrogenaseinarabidopsisthaliana AT masamiyokotahirai novelregulatorymechanismofserinebiosynthesisassociatedwith3phosphoglyceratedehydrogenaseinarabidopsisthaliana
_version_	1718388556751175680

Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana

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