Arabidopsis MAP-Kinase 3 Phosphorylates UDP-Glucose Dehydrogenase a Key Enzyme Providing UDP-Sugar for Cell Wall Biosynthesis

Arabidopsis MAP-Kinase 3 Phosphorylates UDP-Glucose Dehydrogenase : a Key Enzyme Providing UDP-Sugar for Cell Wall Biosynthesis

The enzyme UDP-glucose dehydrogenase (UGD) competes with sucrose-phosphate synthase for the common photosynthesis product UDP-glucose. Sucrose-phosphate synthase is part of a pathway for the export of sucrose from source leaves to neighboring cells or the phloem. UGD is a central enzyme in a pathway...

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Veröffentlicht in:Plant molecular biology reporter. - 1998. - 36(2018), 5 vom: 20., Seite 870-877
1. Verfasser: Kohlberger, Michael (VerfasserIn)
Weitere Verfasser: Thalhamer, Theresa, Weiss, Richard, Tenhaken, Raimund
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Plant molecular biology reporter
Schlagworte:Journal Article Enzyme regulation MAPK Nucleotide sugar biosynthesis UDP-glucose UDP-glucuronic acid
Beschreibung
Zusammenfassung:The enzyme UDP-glucose dehydrogenase (UGD) competes with sucrose-phosphate synthase for the common photosynthesis product UDP-glucose. Sucrose-phosphate synthase is part of a pathway for the export of sucrose from source leaves to neighboring cells or the phloem. UGD is a central enzyme in a pathway for many nucleotide sugars used in local cell wall biosynthesis. Here, we identify a highly conserved phosphorylation site in UGD which is readily phosphorylated by MAP-kinase 3 in Arabidopsis. Phosphorylation occurs at a surface-exposed extra loop in all plant UGDs that is absent in UGDs from bacteria or animals. Phosphorylated sucrose-phosphate synthase is shifted to an inactive form which we did not measure for phosphorylated UGD. Plant UGDs have an extra loop which is phosphorylated by AtMPK3. Phosphorylation is not causing a reduction of UGD activity as found for the competitor enzymes and thus sets a preference for maintaining UDP-sugars at a constant level to prioritize cell wall biosynthesis
Beschreibung:Date Revised 24.07.2024
published: Print-Electronic
Citation Status PubMed-not-MEDLINE
ISSN:0735-9640
DOI:10.1007/s11105-018-1130-y