ReviewBiophysical reviews2018
Identification of UDP-glucose binding site in glycosyltransferase domain of sucrose phosphate synthase from sugarcane (Saccharum officinarum) by structure-based site-directed mutagenesis.
Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Mycorrhizal Fungal Inoculation Reshapes Chemotype, Nutritional Status, and Metabolic Signatures to Enhance Bioactivity inPlants (Basel, Switzerland) · 2026Article
- Arbuscular mycorrhizal fungi mediate leaf sugar profile in water-stressed trifoliate orange.BMC plant biology · 2025Article
- Exogenous tryptophan increases soybean yield by enhancing sucrose-starch metabolism in leaves and seeds at the R6 stage under salt-alkali stress.BMC plant biology · 2025Article
- Suppressing wheat sucrose phosphate synthase 1-B protects wheat against stripe rust.Journal of advanced research · 2025Article
- Current perspectives on the regulatory mechanisms of sucrose accumulation in sugarcane.Heliyon · 2024Review
- The subgenome Saccharum spontaneum contributes to sugar accumulation in sugarcane as revealed by full-length transcriptomic analysis.Journal of advanced research · 2023Article
- Essential Oil Derived from Underutilized PlantsRussian agricultural sciences · 2023Article
- Identification of potential MTAs and candidate genes for juice quality- and yield-related traits in Saccharum clones: a genome-wide association and comparative genomic study.Molecular genetics and genomics : MGG · 2022Article
- Essential oil fromBulletin of the National Research Centre · 2022Article
- Comparative Analysis of Sugar Metabolites and Their Transporters in Sugarcane FollowingInternational journal of molecular sciences · 2021Article
- Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose phosphate synthase.Molecular biology reports · 2021Article
- Article
- Identification of Ginger (Frontiers in genetics · 2020Article
- Foreword to 'Multiscale structural biology: biophysical principles and mechanisms underlying the action of bio-nanomachines', a special issue in Honour of Fumio Arisaka's 70th birthday.Biophysical reviews · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose phosphate synthase (SPS) is believed to be the key enzyme for controlling the biosynthesis of sucrose. SPSs consist of a functional glycosyltransferase domain that shares conserved residues with the glycosyltransferase domain of sucrose biosynthesis-related protein. The formation of sucrose-6-phosphate is catalyzed by SPS with the transfer of a glycosyl group of uridine diphosphate glucose (UDP-G) as an activated donor sugar to a fructose-6-phosphate as a sugar acceptor. However, understanding of the mechanism of catalytic and substrate binding in SPS is very limited. Based on amino acid sequence alignments with several enzymes that belong to the glycosyltransferase family, the UDP-G binding sites that might be critical for catalytic mechanism were identified. Here, we report that single point mutation of R496, D498, and V570 located in the proposed UDP-G binding site led to less active or complete loss of enzyme activity. Through structure-based site-directed mutagenesis and biochemical studies, the results indicated that these residues contribute to the catalytic activity of plant SPS. Moreover, understanding of the UDP-G binding site provides an insight into new strategies for enzyme engineering and redesigning a catalytic mechanism for UDP.
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