ArticleBMC research notes2015
Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms.
Article in BMC research notes, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- CBM20CP, a novel functional protein of starch metabolism in green algae.Plant molecular biology · 2022Article
- Interplay Between the N-Terminal Domains ofFrontiers in plant science · 2021Article
- Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase fromHeliyon · 2020Article
- Molecular dynamics study to improve the substrate adsorption ofAdvances and applications in bioinformatics and chemistry : AABC · 2019Article
- Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis.Frontiers in plant science · 2018Review
- Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri.PloS one · 2018Article
- Starch Synthesis inFrontiers in plant science · 2018Article
- The Importance of Surface-Binding Site towards Starch-Adsorptivity Level inEnzyme research · 2017Review
- Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Cellular and molecular life sciences : CMLS · 2016Review
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Authors and funding
5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundStarch-binding domains are key modules present in several enzymes involved in polysaccharide metabolism. These non-catalytic modules have already been described as essential for starch-binding and the catalytic activity of starch synthase III from the higher plant Arabidopsis thaliana. In Ostreococcus tauri, a unicellular green alga of the Prasinophyceae family, there are three SSIII isoforms, known as Ostta SSIII-A, SSIII-B and SSIII-C.
resultsIn this work, using in silico and in vitro characterization techniques, we have demonstrated that Ostta SSIII-A, SSIII-B and SSIII-C contain two, three and no starch-binding domains, respectively. Additionally, our phylogenetic analysis has indicated that OsttaSSIII-B, presenting three N-terminal SBDs, is the isoform more closely related to higher plant SSIII. Furthermore, the sequence alignment and homology modeling data gathered showed that both the main 3-D structures of all the modeled domains obtained and the main amino acid residues implicated in starch binding are well conserved in O. tauri SSIII starch-binding domains. In addition, adsorption assays showed that OsttaSSIII-A D2 and SSIII-B D2 domains are the two that make the greatest contribution to amylose and amylopectin binding, while OsttaSSIII-B D1 is also important for starch binding.
conclusionsThe results presented here suggest that differences between OsttaSSIII-A and SSIII-B SBDs in the number of and binding of amino acid residues may produce differential affinities for each isoform to polysaccharides. Increasing the knowledge about SBDs may lead to their employment in biomedical and industrial applications.
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