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reductase/càries dental
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Pàgina 1 des de 311 resultats
Targeting the intersubunit cavity of Plasmodium falciparum glutathione reductase by a novel natural inhibitor: computational and experimental evidence.
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Glutathione reductase (GR), a homodimeric FAD-dependent disulfide reductase, is essential for redox homeostasis of the malaria parasite Plasmodium falciparum and has been proposed as an antimalarial drug target. In this study we performed a virtual screening against PfGR, using the structures of
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.
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The chaperonin GroEL binds non-native polypeptides in an open ring via hydrophobic contacts and then, after ATP and GroES binding to the same ring as polypeptide, mediates productive folding in the now hydrophilic, encapsulated cis chamber. The nature of the folding reaction in the cis cavity
Nitrite reductase in Streptoccocus mutans plays a critical role in the survival of this pathogen in oral cavity.
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OBJECTIVE
The mechanisms of nitric oxide (NO) production by bacteria in the oral cavity are still not clearly defined but salivary streptococci have been reported to generate NO. The aim of this study was to clarify the mechanism of nitrite metabolism and generation of NO by Streptococcus mutans, a
Homology Modeling and Probable Active Site Cavity Prediction of Uncharacterized Arsenate Reductase in Bacterial spp
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The arsC gene-encoded arsenate reductase is a vital catalytic enzyme for remediation of environmental arsenic (As). Microorganisms containing the arsC gene can convert pentavalent arsenate (As[V]) to trivalent arsenite (As[III]) to be either retained in the bacterial cell or released into the air.
External loops at the ferredoxin-NADP(+) reductase protein-partner binding cavity contribute to substrates allocation.
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Ferredoxin-NADP(+) reductase (FNR) is the structural prototype of a family of FAD-containing reductases that catalyze electron transfer between low potential proteins and NAD(P)(+)/H, and that display a two-domain arrangement with an open cavity at their interface. The inner part of this cavity
Quantitative measurement of the nitrate reductase activity in the human oral cavity.
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To quantitatively characterise the nitrate reductase activity in the human oral cavity, a new assay based on holding 20 ml of 10 mg nitrate-N/L solution in the mouth was developed. The mouth assay appeared to relate primarily to the oral cavity surface rather than to the saliva. Nitrite formation in
Alkylamine-ligated H93G myoglobin cavity mutant: a model system for endogenous lysine and terminal amine ligation in heme proteins such as nitrite reductase and cytochrome f.
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His93Gly sperm whale myoglobin (H93G Mb) has the proximal histidine ligand removed to create a cavity for exogenous ligand binding, providing a remarkably versatile template for the preparation of model heme complexes. The investigation of model heme adducts is an important way to probe the
Protective effect of salivary nitrate and microbial nitrate reductase activity against caries.
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To test the hypothesis that a combination of high salivary nitrate and high nitrate-reducing capacity are protective against dental caries, 209 children attending the Dental Institute, Barts and The London NHS Trust were examined. Salivary nitrate and nitrite levels, counts of Streptococcus mutans
INTERRELATIONSHIPS AMONG SALIVARY REDUCTASE ACTIVITY, CERTAIN ORAL BACTERIA AND CARIES IN MAN.
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REDUCTASE ACTIVITY OF HUMAN WHOLE SALIVA AS RELATED TO DENTAL CARIES EXPERIENCE. TECHN DOCUM REP NO. SAM-TDR-64-22.
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Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development.
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The malarial parasite Plasmodium falciparum is known to be sensitive to oxidative stress, and thus the antioxidant enzyme glutathione reductase (GR; NADPH+GSSG+H(+) <==> NADP(+)+2 GSH) has become an attractive drug target for antimalarial drug development. Here, we report the 2.6A resolution crystal
A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution.
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The binding of glutathione, some related molecules and two redox compounds to crystals of glutathione reductase has been investigated by X-ray crystallography at 0.3-nm resolution. Models for several bound ligands have been built and subjected to crystallographic refinement. The results clearly show
X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution.
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The crystal structure of the ferredoxin:NADP+ reductase (FNR) from the cyanobacterium Anabaena PCC 7119 has been determined at 2.6 A resolution by multiple isomorphous replacement and refined using 15.0 A to 1.8 A data, collected at 4 degrees C, to an R-factor of 0.172. The model includes 303
Pressure dependence of activity and stability of dihydrofolate reductases of the deep-sea bacterium Moritella profunda and Escherichia coli.
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To understand the pressure-adaptation mechanism of deep-sea enzymes, we studied the effects of pressure on the enzyme activity and structural stability of dihydrofolate reductase (DHFR) of the deep-sea bacterium Moritella profunda (mpDHFR) in comparison with those of Escherichia coli (ecDHFR).
Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: comparison of wild-type protein and active-site mutant D27E.
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To investigate the contribution of solvent environments to the enzymatic function of Escherichia coli dihydrofolate reductase (DHFR), the salt-, pH-, and pressure-dependence of the enzymatic function of the wild-type protein were compared with those of the active-site mutant D27E in relation to
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