Summary of Study ST002810

This data is available at the NIH Common Fund's National Metabolomics Data Repository (NMDR) website, the Metabolomics Workbench, https://www.metabolomicsworkbench.org, where it has been assigned Project ID PR001757. The data can be accessed directly via it's Project DOI: 10.21228/M8M13Z This work is supported by NIH grant, U2C- DK119886.

See: https://www.metabolomicsworkbench.org/about/howtocite.php

This study contains a large results data set and is not available in the mwTab file. It is only available for download via FTP as data file(s) here.

Perform statistical analysis  |  Show all samples  |  Show named metabolites  |  Download named metabolite data  
Download mwTab file (text)   |  Download mwTab file(JSON)   |  Download data files (Contains raw data)
Study IDST002810
Study TitleGAS2 encodes a 2-oxoglutarate dependent dioxygenase involved in ABA catabolism
Study SummaryLiu et al. [1] recently reported the characterization of Arabidopsis thaliana GAS2 (Gain of Function in ABA-modulated Seed Germination 2), which was described as an enzyme that catalyzes the stereospecific hydration of GA12 to produce GA12 16, 17-dihydro-16α-ol (DHGA12). A second paper describes the conversion of GA12 to an unidentified product by GAS2 and also reports that this enzyme does not convert ABA [2]. However, as previously reported [3], we did not find any conversion of [17-14C]-labeled or [1-,7-,12-,18-14C4]-labeled GA12 by GAS2. Instead, we present here data showing that the recombinant GAS2 enzyme is capable of catabolising abscisic acid (ABA) to phaseic acid (PA) and further to a second product, putative 8’-carboxy-ABA (compound A; Fig. 1a) [4]. References: [1] Liu, H. et al. Biosynthesis of DHGA12 and its roles in Arabidopsis seedling establishment. Nat. Commun. 10, 1768 (2019). [2] Xiong, W. et al. The dioxygenase GIM2 functions in seed germination by altering gibberellin production in Arabidopsis. J. Integr. Plant Biol. 60, 276-291 (2018). [3] Lange, T. & Pimenta Lange, M. J. The Multifunctional Dioxygenases of Gibberellin Synthesis. Plant Cell Physiol. 61, 1869-1879 (2020). [4] Lange, T., Atiq, N., Pimenta Lange. GAS2 encodes a 2-oxoglutarate dependent dioxygenase involved in ABA catabolism. bioRxiv, doi: 10.1101/2022.11.16.516706 (2022).
Institute
Technische Universität Braunschweig
DepartmentBiochemie und Physiology der Pflanzen
LaboratoryAG Lange
Last NameLange
First NameTheo
AddressMendelssohnstr. 4
Emailtheo.lange@tu-bs.de
Phone00495313915880
Submit Date2023-08-01
Raw Data AvailableYes
Raw Data File Type(s)raw(Thermo)
Analysis Type DetailGC-MS
Release Date2023-10-11
Release Version1
Theo Lange Theo Lange
https://dx.doi.org/10.21228/M8M13Z
ftp://www.metabolomicsworkbench.org/Studies/ application/zip

Select appropriate tab below to view additional metadata details:


Project:

Project ID:PR001757
Project DOI:doi: 10.21228/M8M13Z
Project Title:Functional GAS2 studies
Project Type:GC-MS qualitative analysis
Project Summary:Liu et al. recently reported the characterization of Arabidopsis thaliana GAS2 (Gain of Function in ABA-modulated Seed Germination 2), which was described as an enzyme that catalyzes the stereospeci?c hydration of GA12 to produce GA12 16, 17-dihydro-16?-ol (DHGA12). A second paper describes the conversion of GA12 to an unidentified product by GAS2 and also reports that this enzyme does not convert ABA. However, as previously reported, we did not find any conversion of [17-14C]-labeled or [1-,7-,12-,18-14C4]-labeled GA12 by GAS2. Instead, we present here data showing that the recombinant GAS2 enzyme is capable of catabolising abscisic acid (ABA) to phaseic acid (PA) and further to a second product, putative 8’-carboxy-ABA (compound A; Fig. 1a).
Institute:Technische Universität Braunschweig
Department:Biochemie und Physiologie der Pflanzen
Laboratory:AG Lange
Last Name:Lange
First Name:Theo
Address:Mendelssohnstr. 4
Email:theo.lange@tu-bs.de
Phone:00495313915880
Contributors:Nadiem Atiq, Maria João Pimenta Lange
  logo