ArticleThe Plant cell2008
The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode.
Article in The Plant cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 65 citations in OpenAlex.
- Comparative study of two xanthan gum glycosyltransferases combining AI structure predictions and molecular modeling.bioRxiv : the preprint server for biology · 2026Article
- Exploring Daptomycin Hypersensitivity inInternational journal of molecular sciences · 2025Article
- Insights into Sucrose Metabolism and Its Ethylene-Dependent Regulation in Cucumis melo L.Molecular biotechnology · 2025Review
- Composition of Proteins Associated with Red Clover (Life (Basel, Switzerland) · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Metabolome profile variations in common bean (Frontiers in genetics · 2023Article
- HPTLC-based fingerprinting: An alternative approach for fructooligosaccharides metabolism profiling.Current research in food science · 2023Article
- Cyanobacteria as cell factories for the photosynthetic production of sucrose.Frontiers in microbiology · 2023Review
- Structural basis for glucosylsucrose synthesis by a member of the α-1,2-glucosyltransferase family.Acta biochimica et biophysica Sinica · 2022Article
- Integrated Degradome and Srna Sequencing Revealed miRNA-mRNA Regulatory Networks between the Phloem and Developing Xylem of Poplar.International journal of molecular sciences · 2022Article
- Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose phosphate synthase.Molecular biology reports · 2021Article
- Transcriptome profiling of non-climacteric 'yellow' melon during ripening: insights on sugar metabolism.BMC genomics · 2020Article
- Freshwater CyanobacteriumApplied and environmental microbiology · 2020Article
- Co-crystal Structure ofFrontiers in microbiology · 2020Article
- Article
- Identification of UDP-glucose binding site in glycosyltransferase domain of sucrose phosphate synthase from sugarcane (Saccharum officinarum) by structure-based site-directed mutagenesis.Biophysical reviews · 2018Review
- Identification and biochemical characterization of WbwB, a novel UDP-Gal: Neu5Ac-R α1,4-galactosyltransferase from the intestinal pathogen Escherichia coli serotype O104.Glycoconjugate journal · 2018Article
- Purification and characterization of recombinant sugarcane sucrose phosphate synthase expressed in E. coli and insect Sf9 cells: an importance of the N-terminal domain for an allosteric regulatory property.Journal of biochemistry · 2016Article
- The Crystal Structure of Nitrosomonas europaea Sucrose Synthase Reveals Critical Conformational Changes and Insights into Sucrose Metabolism in Prokaryotes.Journal of bacteriology · 2015Article
- Sucrose in cyanobacteria: from a salt-response molecule to play a key role in nitrogen fixation.Life (Basel, Switzerland) · 2015Review
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme.
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