hydrolase/dental caries

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Cavities create a potential back door in epoxide hydrolase Rv1938 from Mycobacterium tuberculosis-A molecular dynamics simulation study.

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Mycobacterium tuberculosis (Mtb) is the causative organism of tuberculosis. Extensively drug resistant strains and latency have posed formidable challenges in the treatment of tuberculosis. The current study addresses an alpha/beta hydrolase fold bearing enzyme, epoxide hydrolase Rv1938 from Mtb.

Extracellular Glycoside Hydrolase Activities in the Human Oral Cavity.

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Carbohydrate availability shifts when bacteria attach to a surface and form biofilm. When salivary planktonic bacteria form an oral biofilm, a variety of polysaccharides and glycoproteins are the primary carbon sources; however, simple sugar availabilities are limited due to low diffusion from

Induction of cell infiltration and acid hydrolase release into the peritoneal cavity of mice.

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An injection of thioglycollate into the peritoneal cavity of mice produced a peak of exudate at 4 h, a peak of total leukocytes at 24 h when the predominant cell was the polymorphonuclear neutrophil, and a secondard macrophage phase beginning 2--3 days after thioglycollate. The release of

[The lysosomal hydrolase activity in the blood of patients with inflammatory processes in the parotid gland with surgical pathology of the organs of the abdominal cavity].

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Activities of lysosomal enzymes (acid phosphatase, beta-galactosidase, cathepsin D) were measured in the blood of 38 patients with acute nonepidemic parotitis, caused by surgical diseases of the abdominal organs, and the status of glutathion antioxidant system studied. When appearing in the blood,

Diagnostic potential of lysosomal hydrolases in body cavity effusions.

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Hexosaminidase, alpha-mannosidase, beta-galactosidase, beta-glucuronidase, and arylsulphatase A were measured inperitoneal and pleural effusions from patients with benign, malignant, and inflammatory disorders. Compared with the benign transudates, all enzyme activities were moderately elevated in

How does (E)-2-(acetamidomethylene)succinate bind to its hydrolase? From the binding process to the final result.

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The binding of (E)-2-(acetamidomethylene)succinate (E-2AMS) to E-2AMS hydrolase is crucial for biological function of the enzyme and the last step reaction of vitamin B(6) biological degradation. In the present study, several molecular simulation methods, including molecular docking, conventional

The complex structure of bile salt hydrolase from Lactobacillus salivarius reveals the structural basis of substrate specificity.

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The gut bacterial bile salt hydrolase (BSH) plays a critical role in host lipid metabolism and energy harvest. Therefore, BSH is a promising microbiome target to develop new therapies to regulate obesity in humans and novel non-antibiotic growth promoters for food animals. We previously reported the

An epoxide hydrolase from endophytic Streptomyces shows unique structural features and wide biocatalytic activity

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The genus Streptomyces is characterized by the production of a wide variety of secondary metabolites with remarkable biological activities and broad antibiotic capabilities. The presence of an unprecedented number of genes encoding hydrolytic enzymes with industrial appeal such as epoxide hydrolases

Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.

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Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable

Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets.

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The fatty acid amide hydrolase (FAAH) regulates the endocannabinoid system cleaving primarily the lipid messenger anandamide. FAAH has been well characterized over the years and, importantly, it represents a promising drug target to treat several diseases, including inflammatory-related diseases and

Distribution of microsomal epoxide hydrolase and glutathione S-transferase in the rat olfactory mucosa: relevance to distribution of lesions caused by systemically-administered olfactory toxicants.

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This study represents part an of ongoing effort to understand the mechanism underlying the distribution of the olfactory mucosal lesion resulting from the systemic administration of compounds such as 2,6-dichlorobenzonitrile (dichlobenil) and beta,beta'-iminodipropionitrile (IDPN).

Geotrichum candidum link 1809: hydrolases activity and own method of digestive tract strains biotyping.

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Hydrolase activity of (enzymograms, biotypes) in Geotrichum candidum, one of the poorly described pathogenic fungi, was studied 81 strains were isolated from oral cavity and faeces of patients with gastrointestinal tract disorders. Axenic strains were differentiated with API 20C Aux and API ZYM

Ultrastructure and hydrolase cytochemistry of the developing marmoset yolk sac.

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Yolk sacs from Callithrix jacchus were investigated light and electron microscopically as well as by qualitative light microscopic enzyme histochemistry on days 35 to 126 of gestation. The thin yolk sac wall of the early stages (day 35-41) consists of the cuboid, endodermal epithelium, the

Specific reactions of S-nitrosothiols with cysteine hydrolases: A comparative study between dimethylargininase-1 and CTP synthetase.

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S-Transnitrosation is an important bioregulatory process whereby NO(+) equivalents are transferred between S-nitrosothiols and Cys of target proteins. This reaction proceeds through a common intermediate R-S-N(O(-))-S-R' and it has been proposed that products different from S-nitrosothiols may be

Regulation of prostaglandin synthesis and of the selective release of lysosomal hydrolases by mouse peritoneal macrophages.

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Macrophages isolated from the peritoneal cavity of untreated mice and maintained in tissue culture synthesize and release prostaglandins when challenged with zymosan. These cells also selectively release lysosomal acid hydrolases under the same conditions. The major prostaglandins released into the

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