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trimethylamine/kaaries
Link salvestatakse lõikelauale
Leht 1 alates 26 tulemused
Mechanism of biosynthesis of trimethylamine oxide from choline in the teleost tilapia, Oreochromis niloticus, under freshwater conditions.
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The mechanism of biosynthesis of trimethylamine oxide (TMAO) from dietary precursors in the teleost tilapia (Oreochromis niloticus) was investigated. Diets supplemented with quaternary ammonium choline, glycine betaine, carnitine or phosphatidylcholine were administered and significant increases in
Formation of trimethylamine from dietary choline by Streptococcus sanguis I, which colonizes the mouth.
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Choline is a component of the normal diet, and when humans ingest large amounts they excrete trimethylamine (which can impart a fishy body odor). In the presence of nitrite, trimethylamine can be converted to dimethylnitrosamine, a potent carcinogen. Bacteria in the large intestine metabolize
Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus.
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The periplasmic enzyme dimethyl sulfoxide/trimethylamine N-oxide reductase (DMSOR/TMAOR) from the photosynthetic purple bacterium Rhodobacter capsulatus functions as the terminal electron acceptor in its respiratory chain. The enzyme catalyzes the reduction of highly oxidized substrates like
The Trimethylamine-Formic Acid Complex: Microwave Characterization of a Prototype for Potential Precursors to Atmospheric Aerosol.
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The reactions of amines and carboxylic acids have recently received attention for their possible role in the formation of atmospheric aerosol. Here, we report a microwave study of the trimethylamine-formic acid hydrogen-bonded complex, a simple prototype in which to study amine-carboxylic acid
Effects of feeding diets containing increasing proportions of bunt-infected wheat (Tilletia caries) on performance and health of pigs.
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Tilletia caries is a fungus that mainly infects wheat, causing the disease bunt. Wheat bunt had been one of the most dangerous plant diseases before seed dressing was a common practice. However, it is still of importance in organic farming, since seed dressing is not permitted. Trimethylamine (TMA)
An exposed tyrosine on the surface of trimethylamine dehydrogenase facilitates electron transfer to electron transferring flavoprotein: kinetics of transfer in wild-type and mutant complexes.
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In wild-type trimethylamine dehydrogenase, tyrosine-442 is located at the center of a concave region on the surface of the enzyme that is proposed to form the docking site for the physiological redox acceptor, electron transferring flavoprotein. The intrinsic rate constant for electron transfer in
Trimethylamine and Trimethylamine N-Oxide, a Flavin-Containing Monooxygenase 3 (FMO3)-Mediated Host-Microbiome Metabolic Axis Implicated in Health and Disease.
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Flavin-containing monooxygenase 3 (FMO3) is known primarily as an enzyme involved in the metabolism of therapeutic drugs. On a daily basis, however, we are exposed to one of the most abundant substrates of the enzyme trimethylamine (TMA), which is released from various dietary components by the
How does trimethylamine N-oxide counteract the denaturing activity of urea?
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Trimethylamine N-oxide, TMAO, stabilizes globular proteins and is able to counteract the denaturing activity of urea. The mechanism of this counteraction has remained elusive up to now. A rationalization is proposed grounded on the same theoretical model used to clarify the origin of cold
The Deep Sea Osmolyte Trimethylamine N-Oxide and Macromolecular Crowders Rescue the Antiparallel Conformation of the Human Telomeric G-Quadruplex from Urea and Pressure Stress.
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Organisms are thriving in the deep sea at pressures up to the 1 kbar level, which imposes severe stress on the conformational dynamics and stability of their biomolecules. The impact of osmolytes and macromolecular crowders, mimicking intracellular conditions, on the effect of pressure on the
6-S-cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme.
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Histamine dehydrogenase from Nocardioides simplex is a homodimeric enzyme and catalyzes oxidative deamination of histamine. The gene encoding this enzyme has been sequenced and cloned by polymerase chain reactions and overexpressed in Escherichia coli. The sequence of the complete open reading
Nucleotide-induced folding of cell division protein FtsZ from Staphylococcus aureus.
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The essential bacterial division protein FtsZ uses GTP binding and hydrolysis to assemble into dynamic filaments that treadmill around the Z-ring, guiding septal wall synthesis and cell division. FtsZ is a structural homolog of tubulin and a target for discovering new antibiotics. Here, using FtsZ
Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement.
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One of the proposed roles of the GroEL-GroES cavity is to provide an "infinite dilution" folding chamber where protein substrate can fold avoiding deleterious off-pathway aggregation. Support for this hypothesis has been strengthened by a number of studies that demonstrated a mandatory GroES
Contribution of the surface free energy perturbation to protein-solvent interactions.
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Surface tension measurements were carried out at 20 degrees C by a capillary drop-weight method on aqueous solutions of sodium glutamate (NaGlu), lysine hydrochloride (LysHCl), potassium aspartate (KAsp), arginine hydrochloride (ArgHCl), lysylglutamate (LysGlu), argininylglutamate (ArgGlu),
Postictal spectroscopy and imaging findings mimicking brain tumor recurrence.
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(1)H magnetic resonance spectroscopic imaging (MRSI) was performed on a patient with an admission diagnosis of recurrent astrocytoma. The patient had undergone surgical resection and radiation therapy for a left occipital astrocytoma WHO grade III 12 years previously, and presented with aphasia,
High resolution 1H NMR investigations of the oxidative consumption of salivary biomolecules by ozone: relevance to the therapeutic applications of this agent in clinical dentistry.
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High resolution proton (1H) nuclear magnetic resonance (NMR) spectroscopy was employed to simultaneously evaluate the oxidising actions of ozone (O3) towards a wide range of salivary biomolecules in view of its applications in dental practices, which may serve as a viable and convenient means for
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