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.
Study ID | ST002810 |
Study Title | GAS2 encodes a 2-oxoglutarate dependent dioxygenase involved in ABA catabolism |
Study Summary | Liu 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 |
Department | Biochemie und Physiology der Pflanzen |
Laboratory | AG Lange |
Last Name | Lange |
First Name | Theo |
Address | Mendelssohnstr. 4 |
theo.lange@tu-bs.de | |
Phone | 00495313915880 |
Submit Date | 2023-08-01 |
Raw Data Available | Yes |
Raw Data File Type(s) | raw(Thermo) |
Analysis Type Detail | GC-MS |
Release Date | 2023-10-11 |
Release Version | 1 |
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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 |