The compound identities were verified by mass and retention time matches to authenticated standards (L-asparagine, A0884-25G, Sigma-Aldrich; L-glutamine, G3126-100G, Sigma-Aldrich; L-tryptophan, T8941-25G, Mix Amino acid standard, Sigma-Aldrich; AAS18-5ML, Sigma-Aldrich).
"],"repository":["MetaboLights"],"study_status":["Public"],"ptm_modification":[""],"instrument_platform":["Liquid Chromatography MS - positive - hilic"],"chromatography_protocol":["The amino acid content was analyzed by a QTRAP mass spectrometer (5500, AB Sciex) equipped with UHPLC (ExionLC AD, AB Sciex) and an ACQUITY UPLC BEH Amide column (100mm × 2.1 mm, 1.7 μm, Waters). The injection volume was 1 μL. The mobile phases were composed of 5% acetonitrile/95% water (v/v) (A) and 95% acetonitrile/5% water (v/v) (B), both containing 5 mM ammonium formate and 0.1% formic acid. The column was maintained at 40 °C with a flow rate of 0.3 mL min-1. The gradient of B for the Phe content analysis was as follows: 0 min, 100%; 0.5 min, 100%; 5 min, 85%; 9 min, 40%; 12 min, 40%; 12.1 min, 100%; 15 min, 100%. The gradient of B for the 19 amino acid content analysis was as follows: 0 min, 100%; 1 min, 100%; 17 min, 75%; 19 min, 40%; 20 min, 40%; 20.1 min, 100%; 25 min, 100%.
"],"publication":["A Plastoglobuli-Localized Enzyme Links Phenylalanine Biosynthesis to Translational Homeostasis in Maize."],"submitter_affiliation":["CAS Center for Excellence in Molecular Plant Sciences"],"submitter_name":["Xing Huang"],"organism_part":["endosperm","leaf"],"technology_type":["mass spectrometry assay"],"disease":[""],"extraction_protocol":["Amino acids were extracted from 50 mg of frozen tissue by vortexing for 30 min in 1 mL of ddH2O. After centrifugation (15,000 g, 20 min, 4 °C), transfer 300 µL of supernatant to a new tube. Add 500 µL of methanol: acetonitrile (1:1, v/v), vortex for 3 min, and incubate at –20 °C for 2 h to precipitate proteins. After centrifugation (15,000 g, 20 min, 4 °C), collect 200 µL of supernatant into an insert-equipped vial for analysis.
"],"organism":["Zea mays"],"full_dataset_link":["https://www.ebi.ac.uk/metabolights/MTBLS14852"],"author":["Xing Huang. CAS Center for Excellence in Molecular Plant Sciences. huangxing@cemps.ac.cn.","Yongrui Wu. CAS Center for Excellence in Molecular Plant Sciences. yrwu@cemps.ac.cn."],"data_transformation_protocol":["Instrument control and data acquisition were performed using Analyst 1.7.2 software (AB SCIEX), and data processing was performed using MultiQuant 3.0.3 software (AB SCIEX).
"],"study_factor":["Plant part"],"submitter_email":["huangxing@cemps.ac.cn"],"sample_collection_protocol":["The different genotype plant stem were collected in the heading stage and immediately frozen in liquid nitrogen. The stem was then ground into fine powder. The 18-DAP B104 and adt2.2 endosperm were collected and immediately frozen in liquid nitrogen. The endosperm was then ground into fine powder.
"],"omics_type":["Metabolomics"],"study_design":["Metabolomics","Zea mays","targeted analysis","SCIEX ExionLC AD","ADT2.2","liquid chromatography-tandem mass spectrometry","experimental blank","AB SCIEX QTRAP 5500","Maize","endosperm","leaf"],"curator_keywords":["Metabolomics","Zea mays","targeted analysis","SCIEX ExionLC AD","ADT2.2","liquid chromatography-tandem mass spectrometry","experimental blank","AB SCIEX QTRAP 5500","Maize","endosperm","leaf"],"mass_spectrometry_protocol":["All analytes were detected using Multiple Reaction Monitoring (MRM) mode. The optimized ESI operating parameters for positive mode were: ion spray voltage, 5.5 kV; ion spray temperature, 500 °C; curtain gas, 35 psi; ion source gas 1, 50psi; ion source gas 2, 50 psi.
"],"metabolite_name":["Tyrosine","Glutamic acid","Alanine","Phenylalanine","Threonine","Serine","Methionine","Tryptophan","Proline","Leucine","Glycine","Histidine","Arginine","Lysine","Valine","Asparagine","Aspartic acid","Glutamine","Isoleucine"],"additional_accession":[]},"is_claimable":false,"name":"A Plastoglobuli-Localized Enzyme Links Phenylalanine Biosynthesis to Translational Homeostasis in Maize","description":"Aromatic amino acids are essential precursors for numerous plant metabolites, with phenylalanine (Phe) forming the basis of the phenylpropanoid pathway. Here, we reveal a critical mechanism for Phe biosynthesis in maize, demonstrating that all seven arogenate dehydratases (ADTs) are specifically localized to plastoglobuli (PGs) in chloroplasts, and ADT2.2 shows high catalytic activity towards arogenate and prephenate. This discovery establishes PGs as a site for Phe synthesis. Genetic analysis confirms that only ADT2.2 is indispensable for plant and seed development, with its loss causing a severe Phe deficiency in seeds. This metabolic blockage directly reduced the tRNAPhe-GAA charging, thereby repressing protein translation. Crucially, we uncover that Phe starvation disproportionately affects the decoding efficiency of wobble-paired codons, increasing ribosome pausing. Our work provides biochemical and genetic evidence that PGs-localized ADT2.2 catalyzes Phe synthesis and reveals a link between amino acid availability and codon-specific translation dynamics.","dates":{"publication":"2026-06-25","submission":"2026-06-24"},"accession":"MTBLS14852","cross_references":{"MetaboLights":["MTBLC32861"],"ChEBI":["CHEBI:32861"]}}