ArticleFrontiers in plant science2019
Spermidine Synthase (SPDS) Undergoes Concerted Structural Rearrangements Upon Ligand Binding - A Case Study of the Two SPDS Isoforms From
Article in Frontiers in plant science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Putrescine-bound structure and multi-temperature crystallography provide new insights into ligand binding and conformational heterogeneity in spermidine synthase.Structural dynamics (Melville, N.Y.) · 2026Article
- Crystal structure of apo human spermidine synthase reveals dynamic rearrangement at the active site.Structural dynamics (Melville, N.Y.) · 2026Article
- Molecular dynamics simulation analysis of a modelled spermidine synthase fromBioinformation · 2025Article
- Structural Analysis of Spermidine Synthase fromMolecules (Basel, Switzerland) · 2023Article
- S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.International journal of biological macromolecules · 2020Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Spermidine synthases (SPDSs) catalyze the production of the linear triamine, spermidine, from putrescine. They utilize decarboxylated S-adenosylmethionine (dc-SAM), a universal cofactor of aminopropyltransferases, as a donor of the aminopropyl moiety. In this work, we describe crystal structures of two SPDS isoforms from
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