putrescine/cariës

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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

Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.

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Putrescine, 1,4-diaminobutane, is an intermediate in the biosynthesis of more complexed polyamines, spermidine and spermine. Unlike other eukaryotes, plants have evolved a multistep pathway for putrescine biosynthesis that utilizes arginine. In the final reaction, N-carbamoylputrescine is hydrolyzed

Polyamines of dental plaque in caries-resistant vs. caries-susceptible adults.

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Utilizing a sensitive liquid chromatographic system, polyamines were quantitated in three-day plaque from 13 caries-resistant (CR) and 35 caries-susceptible (CS) adults after they had fasted for 12 hours. The values for putrescine and cadaverine were significantly higher in the CR group. This may be

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

Structure-based redesign of cofactor binding in putrescine oxidase.

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Putrescine oxidase (PuO) from Rhodococcus erythropolis is a soluble homodimeric flavoprotein, which oxidizes small aliphatic diamines. In this study, we report the crystal structures and cofactor binding properties of wild-type and mutant enzymes. From a structural viewpoint, PuO closely resembles

Integrated analyses utilizing metabolomics and transcriptomics reveal perturbation of the polyamine pathway in oral cavity squamous cell carcinoma.

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Oral cavity squamous cell carcinoma (OSCC), the most common malignancy of the oral cavity, is associated with poor prognosis and high mortality worldwide. Moreover, knowledge of the metabolic alterations that occur in OSCC is still limited. In the present study, we used a quantitative metabolomic

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

Occurence of Veillonella and Neisseria in the niches of the human oral cavity.

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Samples collected from the dental surface, gingival sulcus, dorsum of the tongue and from the cheek of ten adults (18 to 32 years) were investigated to identify the Veillonella and Neisseria species present by applying the taxonomic criteria suggested in the latest edition of Bergey's Manual. The

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

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

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

Transglutaminase expression in rat parotid gland after isoproterenol stimulation.

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Transglutaminases (E.C. 2.3.2.13) are calcium-dependent enzymes that catalyze the covalent cross-linking of proteins, and occur in multiple molecular forms in a variety of tissues. Distribution of each form of transglutaminase varies with different tissues. Studies were undertaken to characterize

An important lysine residue in copper/quinone-containing amine oxidases.

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The interaction of xenon with copper/6-hydroxydopa (2,4,5-trihydroxyphenethylamine) quinone (TPQ) amine oxidases from the plant pulses lentil (Lens esculenta) and pea (Pisum sativum) (seedlings), the perennial Mediterranean shrub Euphorbia characias (latex), and the mammals cattle (serum) and pigs

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