ArticlePloS one2016
Characterization of the Sucrose Phosphate Phosphatase (SPP) Isoforms from Arabidopsis thaliana and Role of the S6PPc Domain in Dimerization.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 19 citations in OpenAlex.
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- Organic fertilizer substitution altered the waxy maize grain quality and aroma volatiles formation by the integrated transcriptomic and metabolomic analyses.Frontiers in plant science · 2025Article
- Current perspectives on the regulatory mechanisms of sucrose accumulation in sugarcane.Heliyon · 2024Review
- Cyanobacteria as cell factories for the photosynthetic production of sucrose.Frontiers in microbiology · 2023Review
- Meta-analysis highlights the key drought responsive genes in genes: PEPC and TaSAG7 are hubs response networks.Journal, genetic engineering & biotechnology · 2022Article
- Mobile forms of carbon in trees: metabolism and transport.Tree physiology · 2022Review
- Transcription Profiles Reveal Age-Dependent Variations of Photosynthetic Properties and Sugar Metabolism in Grape Leaves (International journal of molecular sciences · 2022Article
- Sucrose-phosphate phosphatase from sugarcane reveals an ancestral tandem duplication.BMC plant biology · 2021Article
- Unraveling the Genome of a High Yielding Colombian Sugarcane Hybrid.Frontiers in plant science · 2021Article
- The Starch Is (Not) Just Another Brick in the Wall: The Primary Metabolism of Sugars During Banana Ripening.Frontiers in plant science · 2019Review
- Sucrose metabolism in developing oil-rich tubers of Cyperus esculentus: comparative transcriptome analysis.BMC plant biology · 2018Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Sucrose-phosphate phosphatase (SPP) catalyses the final step in the sucrose biosynthesis pathway. Arabidopsis thaliana genome codifies four SPP isoforms. In this study, the four Arabidopsis thaliana genes coding for SPP isoforms have been cloned, expressed in Escherichia coli and the kinetic and regulatory properties of the purified enzymes analysed. SPP2 is the isoform showing the highest activity, with SPP3b and SPP3a showing lower activity levels. No activity was detected for SPP1. We propose that this lack of activity is probably due to the absence of an essential amino acid participating in catalysis and/or in the binding of the substrate, sucrose-6-phosphate (Suc6P). The expression patterns of Arabidopsis SPP genes indicate that SPP2 and SPP3b are the main isoforms expressed in different tissues and organs, although the non-catalytic SPP1 is the main isoform expressed in roots. Thus, SPP1 could have acquired new unknown functions. We also show that the three catalytically active SPPs from Arabidopsis are dimers. By generating a chimeric SPP composed of the monomeric cyanobacterial SPP fused to the higher plant non-catalytic S6PPc domain (from SPP2), we show that the S6PPc domain is responsible for SPP dimerization. This is the first experimental study on the functionality and gene expression pattern of all the SPPs from a single plant species.
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