ArticleThe Journal of biological chemistry2008
Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 119 citations in OpenAlex.
- Branched-chain polyamines: evolutionary adaptation and biotechnological potential.Amino acids · 2026Review
- Crystal structure of apo human spermidine synthase reveals dynamic rearrangement at the active site.Structural dynamics (Melville, N.Y.) · 2026Article
- Architecture of the human KICSTOR and GATOR1-KICSTOR complexes.Nature structural & molecular biology · 2025Article
- Spermine synthase in Snyder-Robinson syndrome and cancer.Molecular biology reports · 2025Review
- Multi-Temperature Crystallography of S-Adenosylmethionine Decarboxylase Observes Dynamic Loop Motions.Biomolecules · 2025Article
- Molecular dynamics simulation analysis of a modelled spermidine synthase fromBioinformation · 2025Article
- Structural Insights into the Mechanisms Underlying Polyaminopathies.International journal of molecular sciences · 2024Review
- Snyder-Robinson syndrome presenting with learning disability, epilepsy, and osteoporosis: a novelRare (Amsterdam, Netherlands) · 2024Article
- Polyamines: their significance for maintaining health and contributing to diseases.Cell communication and signaling : CCS · 2023Review
- Difluoromethylornithine rebalances aberrant polyamine ratios in Snyder-Robinson syndrome.EMBO molecular medicine · 2023Article
- c-MYC-Driven Polyamine Metabolism in Ovarian Cancer: From Pathogenesis to Early Detection and Therapy.Cancers · 2023Review
- Overexpression of SMS in the tumor microenvironment is associated with immunosuppression in hepatocellular carcinoma.Frontiers in immunology · 2022Article
- METTL3-IGF2BP3-axis mediates the proliferation and migration of pancreatic cancer by regulating spermine synthase m6A modification.Frontiers in oncology · 2022Article
- Novel Hemizygous Missense Variant of Spermine Synthase (Molecular syndromology · 2021Article
- Whole-exome sequencing identifies a novel mutation in spermine synthase gene (SMS) associated with Snyder-Robinson Syndrome.BMC medical genetics · 2020Article
- Article
- Myosin Va and spermine synthase: partners in exosome transport.Bioscience reports · 2019Article
- Myosin Va interacts with the exosomal protein spermine synthase.Bioscience reports · 2019Article
- DFMD: Fast and Effective DelPhiForce Steered Molecular Dynamics Approach to Model Ligand Approach Toward a Receptor: Application to Spermine Synthase Enzyme.Frontiers in molecular biosciences · 2019Article
- Polyamines in Microalgae: Something Borrowed, Something New.Marine drugs · 2018Review
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
The crystal structures of two ternary complexes of human spermine synthase (EC 2.5.1.22), one with 5'-methylthioadenosine and spermidine and the other with 5'-methylthioadenosine and spermine, have been solved. They show that the enzyme is a dimer of two identical subunits. Each monomer has three domains: a C-terminal domain, which contains the active site and is similar in structure to spermidine synthase; a central domain made up of four beta-strands; and an N-terminal domain with remarkable structural similarity to S-adenosylmethionine decarboxylase, the enzyme that forms the aminopropyl donor substrate. Dimerization occurs mainly through interactions between the N-terminal domains. Deletion of the N-terminal domain led to a complete loss of spermine synthase activity, suggesting that dimerization may be required for activity. The structures provide an outline of the active site and a plausible model for catalysis. The active site is similar to those of spermidine synthases but has a larger substrate-binding pocket able to accommodate longer substrates. Two residues (Asp(201) and Asp(276)) that are conserved in aminopropyltransferases appear to play a key part in the catalytic mechanism, and this role was supported by the results of site-directed mutagenesis. The spermine synthase.5'-methylthioadenosine structure provides a plausible explanation for the potent inhibition of the reaction by this product and the stronger inhibition of spermine synthase compared with spermidine synthase. An analysis to trace possible evolutionary origins of spermine synthase is also described.
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