ArticleFrontiers in plant science2018
Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) From
Article in Frontiers in plant science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Genomic diversification between aposematic and cryptic phenotypes of Oophaga granulifera (Anura: Dendrobatidae).Scientific reports · 2026Article
- Evaluating the Impact of Two Different Diets on the Protein Profile of the Brain, Liver, and Intestine of the Barramundi.Proteomes · 2026Article
- Insights of cellular and molecular changes in sugarcane response to oxidative signaling.BMC plant biology · 2025Article
- Overexpression of Phosphoserine Aminotransferase (Plants (Basel, Switzerland) · 2024Article
- Constructing and interpreting a large-scale variant effect map for an ultrarare disease gene: Comprehensive prediction of the functional impact of PSAT1 genotypes.PLoS genetics · 2023Article
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
- Molecular Structure of Phosphoserine Aminotransferase fromInternational journal of molecular sciences · 2023Article
- Lipid and Protein Oxidation of Brown Rice and Selenium-Rich Brown Rice during Storage.Foods (Basel, Switzerland) · 2022Article
- Over-Expression of Phosphoserine Aminotransferase-Encoding Gene (International journal of molecular sciences · 2022Article
- Metabolic alterations in algaEnvironmental science. Nano · 2022Article
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- L-serine synthesis via the phosphorylated pathway in humans.Cellular and molecular life sciences : CMLS · 2020Review
- Structural Study of Agmatine Iminohydrolase FromFrontiers in plant science · 2019Article
- Spermidine Synthase (SPDS) Undergoes Concerted Structural Rearrangements Upon Ligand Binding - A Case Study of the Two SPDS Isoforms FromFrontiers in plant science · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Phosphoserine aminotransferase (PSAT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the conversion of 3-phosphohydroxypyruvate (3-PHP) to 3-phosphoserine (PSer) in an L-glutamate (Glu)-linked reversible transamination reaction. This process proceeds through a bimolecular ping-pong mechanism and in plants takes place in plastids. It is a part of the phosphorylated pathway of serine biosynthesis, one of three routes recognized in plant organisms that yield serine. In this three-step biotransformation, 3-phosphoglycerate (3-PGA) delivered from plastidial glycolysis and Calvin cycle is oxidized by 3-PGA dehydrogenase. Then, 3-PHP is subjected to transamination with Glu to yield PSer and α-ketoglutarate (AKG). In the last step of the pathway, serine is produced by the action of phosphoserine phosphatase. Here we present the structural characterization of PSAT isoform 1 from
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