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spermidine/karijes
Veza se sprema u međuspremnik
Page 1 od 28 rezultati
Femtomolar Detection of Spermidine using Au Decorated SiO2 Nanohybrid on Plasmon-Coupled Extended Cavity Nanointerface: A Smartphone based Fluorescence Dequenching approach.
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Coupling of photons with molecular emitters in different nanocavities have resulted in transformative plasmonic applications. The rapidly expanding field of surface plasmon-coupled emission (SPCE) has synergistically employed subwavelength optical properties of localized surface plasmon resonance
The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor.
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Polyamines are essential in all branches of life. Spermidine synthase (putrescine aminopropyltransferase, PAPT) catalyzes the biosynthesis of spermidine, a ubiquitous polyamine. The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution in the presence
Carcinogenicity in Syrian golden hamsters of N-nitrosamines formed during nitrosation of spermidine.
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Several N-nitrosamines are formed during the nitrosation of the polyamines, spermidine and spermine. Since these polyamines may represent a source for the endogenous or exogenous formation of N-nitrosamines, their major nitrosation products were assayed for carcinogenicity in male Syrian golden
A novel inhibitor of Plasmodium falciparum spermidine synthase: a twist in the tail.
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BACKGROUND
Plasmodium falciparum is the most pathogenic of the human malaria parasite species and a major cause of death in Africa. It's resistance to most of the current drugs accentuates the pressing need for new chemotherapies. Polyamine metabolism of the parasite is distinct from the human
Putrescine or spermidine binding site of aminopropyltransferases and competitive inhibitors.
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A model of the active site of aminopropyltransferases was proposed based on the study of a number of monoamino and diamino compounds as potential inhibitors and substrates, respectively, of spermidine synthase purified from pig liver. The active site seems to have a relatively large hydrophobic
Polyamine metabolism in carcinoma of the oral cavity compared with adjacent and normal oral mucosa.
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In this study, polyamine biosynthesis required for cellular proliferation showed elevated levels in neoplastic cells. Putrescine, spermidine, and spermine, as well as the rate-limiting enzyme ornithine decarboxylase, were measured to evaluate differences in tissue concentration in squamous cell
[Polyamines in tumors of the oral cavity].
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The polyamines putrescine, spermidine and spermine are essential for normal growth and differentiation and the activity of the enzymes participating in their synthesis and catabolism are markedly modified in actively proliferating cells in vitro and in vivo. In some neoplastic cells a good
Molecular mechanism underlying promiscuous polyamine recognition by spermidine acetyltransferase.
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Spermidine acetyltransferase (SAT) from Escherichia coli, which catalyses the transfer of acetyl groups from acetyl-CoA to spermidine, is a key enzyme in controlling polyamine levels in prokaryotic cells. In this study, we determined the crystal structure of SAT in complex with spermidine (SPD) and
Evolution of the key alkaloid enzyme putrescine N-methyltransferase from spermidine synthase.
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Putrescine N-methyltransferases (PMTs) are the first specific enzymes of the biosynthesis of nicotine and tropane alkaloids. PMTs transfer a methyl group onto the diamine putrescine from S-adenosyl-l-methionine (SAM) as coenzyme. PMT proteins have presumably evolved from spermidine synthases
Investigations about N-aminopropyl transferases probably involved in biomineralization.
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Polyamines are widespread distributed all over in living organisms. In Thalassiosira pseudonana 10 N-aminopropyl transferase like nucleotide sequences exists. It is assumed that these sequences are involved in the biomineralization of the diatom shell. The cDNA of the sequences were cloned,
Active site geometry of a novel aminopropyltransferase for biosynthesis of hyperthermophile-specific branched-chain polyamine.
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Branched-chain polyamines are found exclusively in thermophilic bacteria and Euryarchaeota and play essential roles in survival at high temperatures. In the present study, kinetic analyses of a branched-chain polyamine synthase from the hyperthermophilic archaeon Thermococcus kodakarensis (Tk-BpsA)
Resembling breast milk: influence of polyamine-supplemented formula on neonatal BALB/cOlaHsd mouse microbiota.
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Infant microbiota is influenced by numerous factors, such as delivery mode, environment, prematurity and diet (breast milk or formula). In addition to its nutritional value, breast milk contains bioactive substances that drive microbial colonisation and support immune system development, which are
Actinomyces weissii sp. nov., isolated from dogs.
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Two Gram-positive, rod-shaped, non-spore-forming bacteria were isolated from the oral cavities of two dogs. On the basis of 16S rRNA gene sequence similarities both strains were shown to belong to the genus Actinomyces and were most closely related to Actinomyces bovis (97.3% and 97.5%,
Vesicle formed by amphiphilc cucurbit[6]uril: versatile, noncovalent modification of the vesicle surface, and multivalent binding of sugar-decorated vesicles to lectin.
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We report a novel vesicle formed by an amphiphilic CB[6] derivative, the surface of which can be easily modified via host-guest interactions by taking advantage of molecular cavities, readily accessible at the vesicle surface, and their strong affinity toward polyamines. Amphiphilic CB[6] derivative
Study on the Binding Interaction of the α,α',δ,δ'-Tetramethylcucurbit[6]uril With Biogenic Amines in Solution and the Solid State.
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1H NMR spectroscopy and MALDI-TOF mass spectrometry were utilized to examine the binding interaction of α,α',δ,δ'-tetramethylcucurbit[6]uril (TMeQ[6]) and six biogenic amines (spermine, spermidine, 2-phenethylamine, tyramine, histamine, and tryptamine). Their 1H NMR spectra both at pD = 7 and pD = 3
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