ArticleThe Journal of biological chemistry2008
Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- A role of protein conformational dynamics in mammalian DNA methylation.Structural dynamics (Melville, N.Y.) · 2026Review
- RNA triphosphatase-mediated mRNA capping is essential for maintaining transcript homeostasis and the survival of Toxoplasma gondii.Nature communications · 2025Article
- Deep learning network for NMR spectra reconstruction in time-frequency domain and quality assessment.Nature communications · 2025Article
- Two triphosphate tunnel metalloenzymes from apple exhibit adenylyl cyclase activity.Frontiers in plant science · 2022Article
- Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes.Biomolecules · 2021Review
- Triphosphate Tunnel Metalloenzyme Function in Senescence Highlights a Biological Diversification of This Protein Superfamily.Plant physiology · 2017Article
- mRNA capping: biological functions and applications.Nucleic acids research · 2016Review
- Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.The Journal of biological chemistry · 2015Article
- Thiamine triphosphate: a ubiquitous molecule in search of a physiological role.Metabolic brain disease · 2014Review
- Arabidopsis triphosphate tunnel metalloenzyme2 is a negative regulator of the salicylic acid-mediated feedback amplification loop for defense responses.Plant physiology · 2014Article
- High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved.PloS one · 2012Article
- A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism.The Journal of biological chemistry · 2011Article
- Thiamine status in humans and content of phosphorylated thiamine derivatives in biopsies and cultured cells.PloS one · 2010Article
- Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme.The Journal of biological chemistry · 2008Article
- Automated error-tolerant macromolecular structure determination from multidimensional nuclear Overhauser enhancement spectra and chemical shift assignments: improved robustness and performance of the PASD algorithm.Journal of biomolecular NMR · 2008Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Mammalian soluble thiamine triphosphatase (ThTPase) is a 25-kDa cytosolic enzyme that specifically catalyzes the conversion of thiamine triphosphate (ThTP) to thiamine diphosphate and has an absolute requirement for divalent cations. We have investigated the kinetic properties of recombinant mouse thiamine triphosphatase (mThTPase) and determined its solution structure by NMR spectroscopy. Residues responsible for binding Mg(2+) and ThTP were determined from NMR titration experiments. The binding of Mg(2+) induced only a minor local conformational change, whereas ThTP binding was found to cause a more global conformational change. We derived a structural model for the mThTPase.ThTP.Mg(2+) ternary complex and concluded from this that whereas free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold. Our results provide a functional rationale for a number of conserved residues and suggest an essential role for Mg(2+) in catalysis. We propose a mechanism underlying the high substrate specificity of mThTPase and discuss the possible role of water molecules in enzymatic catalysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.