Chondroitinases and Chondroitin Lyases
Carbon Monoxide Poisoning
Molecular Sequence Data
Amino Acid Sequence
Oxidoreductases Acting on Sulfur Group Donors
Chemical Warfare Agents
Chondroitin ABC Lyase
Sequence Homology, Amino Acid
Sequence Analysis, DNA
Gene Expression Regulation, Bacterial
RNA, Ribosomal, 16S
Carbon Compounds, Inorganic
Sulfur Group Transferases
Electrophoresis, Polyacrylamide Gel
DNA-(Apurinic or Apyrimidinic Site) Lyase
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Oceans and Seas
Metabolic Networks and Pathways
Magnetic Resonance Spectroscopy
Heating garlic inhibits its ability to suppress 7, 12-dimethylbenz(a)anthracene-induced DNA adduct formation in rat mammary tissue. (1/405)The present studies compared the impact of heating, either by microwave or convection oven, on the ability of garlic to reduce the in vivo bioactivation of 7,12-dimethylbenz(a)anthracene (DMBA) in 55-d-old female Sprague-Dawley rats. In study 1, rats were fed a semipurified casein-based diet and treated by gastric gavage thrice weekly for 2-wk with crushed garlic (0.7 g in 2 mL corn oil) or the carrier prior to DMBA treatment (50 mg/kg body weight). Providing crushed garlic reduced by 64% (P < 0.05) the quantity DMBA-induced DNA adducts present in mammary epithelial cells compared to controls. In study 2, microwave treatment for 60 s, but not 30 s, decreased (P < 0.05) the protection provided by garlic against DMBA-induced adduct formation. In study 3, allowing crushed garlic to stand for 10 min prior to microwave heating for 60 s significantly (P < 0.05) restored its anticarcinogenic activity. Microwave heating of garlic for 30 s resulted in a 90% loss of alliinase activity. Heating in a convection oven (study 4) also completely blocked the ability of uncrushed garlic to retard DMBA bioactivation. Study 5 revealed that providing either 0.105 micromol diallyl disulfide or S-allyl cysteine by gastric gavage thrice weekly for 2 wk was effective in retarding DMBA bioactivation but isomolar alliin was not. These studies provide evidence that alliinase may be important for the formation of allyl sulfur compounds that contribute to a depression in DMBA metabolism and bioactivation. (+info)
Hyperproduction of recombinant ferredoxins in escherichia coli by coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hs cA-fdx-ORF3 gene cluster. (2/405)Fe-S proteins acquire Fe-S clusters by an unknown post-translational mechanism. To study the in vivo synthesis of the Fe-S clusters, we constructed an experimental system to monitor the expressed ferredoxin (Fd) as a reporter of protein-bound Fe-S clusters assembled in Escherichia coli. Overexpression of five Fds in a T7 polymerase-based system led to the formation of soluble apoFds and mature holoFds, indicating that assembly of the Fe-S cluster into apoFd polypeptides is a rate-limiting step. We examined the coexpression of the E. coli ORF1-ORF2-iscS-iscU-iscA-hscB-hsc A-fdx-ORF3 gene cluster, which has recently been suggested to be involved in the formation or repair of Fe-S protein [Zheng, L., Cash, V.L., Flint, D.H., and Dean, D.R. (1998) J. Biol. Chem. 273, 13264-13272], with reporter Fds using compatible plasmids. The production of all five reporter holoFds examined was dramatically increased by the coexpression of the gene cluster, and apparent specificity to the polypeptides or to the type of Fe-S clusters was not observed. The increase in holoFd production was observed under the coexpression conditions in all culture media examined, with either 2 x YT medium or Terrific broth, and with or without supplemental cysteine or iron. These results indicate that the proteins encoded by the gene cluster are involved in the assembly of the Fe-S clusters in a wide variety of Fe-S proteins. (+info)
Glutathione-dependent metabolism of cis-3-(9H-purin-6-ylthio)acrylic acid to yield the chemotherapeutic drug 6-mercaptopurine: evidence for two distinct mechanisms in rats. (3/405)cis-3-(9H-Purin-6-ylthio)acrylic acid (PTA) is a structural analog of azathioprine, a prodrug of the antitumor and immunosuppressive drug 6-mercaptopurine (6-MP). In this study, we examined the in vitro and in vivo metabolism of PTA in rats. Two metabolites of PTA, 6-MP and the major metabolite, S-(9H-purin-6-yl)glutathione (PG), were formed in a time- and GSH-dependent manner in vitro. Formation of 6-MP and PG occurred nonenzymatically, but 6-MP formation was enhanced 2- and 7-fold by the addition of liver and kidney homogenates, respectively. Purified rat liver glutathione S-transferases enhanced 6-MP formation from PTA by 1.8-fold, whereas human recombinant alpha, mu, and pi isozymes enhanced 6-MP formation by 1.7-, 1.3-, and 1.3-fold, respectively. In kidney homogenate incubations, PG accumulation was only observed during the first 15 min because of further metabolism by gamma-glutamyltranspeptidase, dipeptidase, and beta-lyase to yield 6-MP, as indicated by the use of the inhibitors acivicin and aminooxyacetic acid. Based on these results and other lines of evidence, two different GSH-dependent pathways are proposed for 6-MP formation: an indirect pathway involving PG formation and further metabolism to 6-MP, and a direct pathway in which PTA acts as a Michael acceptor. HPLC analyses of urine of rats treated i.p. with PTA (100 mg/kg) showed that 6-MP was formed in vivo and excreted in urine without apparent liver or kidney toxicity. Collectively, these studies show that PTA is metabolized to 6-MP both in vitro and in vivo and may therefore be a useful prodrug of 6-MP. (+info)
Efficacy of recombinant methioninase in combination with cisplatin on human colon tumors in nude mice. (4/405)The present treatment of colon cancer is based on 5-fluorouracil (5-FU). Despite promising results of combining leucovorin or levamisole with 5-FU, the 5-year survival rate of patients with advanced colon cancer has not increased significantly. Colon tumors in vitro have been shown previously to have an elevated requirement for methionine, suggesting a new therapeutic target. In this study, targeting the methionine dependence of colon tumors is effected by recombinant methioninase (rMETase), alone and in combination with cisplatin (CDDP). In vitro results demonstrated that CDDP and rMETase act synergistically on the human colon cancer cell line SW 620, with a combination index (CI) of 0.45, as well as on the human colon cancer cell line Colo 205 with a CI of 0.7. Human colon cancer lines HCT 15, HT 29, Colo 205, and SW 620 growing in nude mice were treated with rMETase to determine an effective dose for depletion of tumor methionine. rMETase at 15 units/g/day for 5 days depleted tumor methionine in all four tumor types to approximately 30% of untreated control. rMETase alone arrested growth of HCT 15 and HT29 in nude mice for 1 week after treatment termination. Colo 205 and SW 620 were partially arrested by rMETase. However, CDDP in combination with rMETase resulted in tumor regression of Colo 205 and growth arrest of SW 620 in nude mice. The ratio of the treated:control group (T:C) tumor weights for Colo 205 was 8% when CDDP was given on day-5, followed by treatment on days 5-9 with rMETase. This treatment schedule resulted in two of the six animals having no detectable tumor when the experiment was terminated on day 16. SW620 was resistant to CDDP alone and only partially sensitive to rMETase alone. However, when SW 620 was treated with rMETase from days-5 to -9 and CDDP on day-5, tumor growth was arrested. The results demonstrate that rMETase used simultaneously in combination with CDDP had significant antitumor efficacy in colon cancer in vitro and in vivo. The data suggest a novel and promising therapeutic approach by targeting the elevated methionine dependence of colon cancer. (+info)
Metabolism of acrylate to beta-hydroxypropionate and its role in dimethylsulfoniopropionate lyase induction by a salt marsh sediment bacterium, Alcaligenes faecalis M3A. (5/405)Dimethylsulfoniopropionate (DMSP) is degraded to dimethylsulfide (DMS) and acrylate by the enzyme DMSP lyase. DMS or acrylate can serve as a carbon source for both free-living and endophytic bacteria in the marine environment. In this study, we report on the mechanism of DMSP-acrylate metabolism by Alcaligenes faecalis M3A. Suspensions of citrate-grown cells expressed a low level of DMSP lyase activity that could be induced to much higher levels in the presence of DMSP, acrylate, and its metabolic product, beta-hydroxypropionate. DMSP was degraded outside the cell, resulting in an extracellular accumulation of acrylate, which in suspensions of citrate-grown cells was then metabolized at a low endogenous rate. The inducible nature of acrylate metabolism was evidenced by both an increase in the rate of its degradation over time and the ability of acrylate-grown cells to metabolize this molecule at about an eight times higher rate than citrate-grown cells. Therefore, acrylate induces both its production (from DMSP) and its degradation by an acrylase enzyme. (1)H and (13)C nuclear magnetic resonance analyses were used to identify the products resulting from [1-(13)C]acrylate metabolism. The results indicated that A. faecalis first metabolized acrylate to beta-hydroxypropionate outside the cell, which was followed by its intracellular accumulation and subsequent induction of DMSP lyase activity. In summary, the mechanism of DMSP degradation to acrylate and the subsequent degradation of acrylate to beta-hydroxypropionate in the aerobic beta-Proteobacterium A. faecalis has been described. (+info)
Beta-cyanoalanine synthase: purification and characterization. (6/405)Beta-cyano-L-alanine synthase [L-cysteine hydrogen-sulfide-lyase (adding HCN), EC 126.96.36.199] was purified about 4000-fold from blue lupine seedlings. The enzyme was homoegeneous on gel electrophoresis and free of contamination by other pyridoxal-P-dependent lyases. The enzyme has a molecular weight of 52,000 and contains 1 mole of pyridoxal-P per mole of protein; its isoelectric point is situated at pH 4.7. Its absorption spectrum has two maxima, at 280 and 410 nm. L-Cysteine is the natural primary (amino acid) substrate; beta-chloro- and beta-thiocyano can serve (with considerably lower affinity) instead of cyanide as cosubstrates for cyanoalanine synthase. The synthase is refractory to DL-cycloserine and D-penicillamine, potent inhibitors of many pyridoxal-P-dependent enzymes. Cyanoalanine synthase catalyzes slow isotopic alpha-H exchange in cysteine and in end-product amino acids; the rates of alpha-H exchange in nonreacted (excess) cysteine are markedly increased in the presence of an adequate cosubstrate; no exchange is observed of H atoms in beta-position. (+info)
Cloning, expression, and cellular localization of a human prenylcysteine lyase. (7/405)Prenylated proteins contain either a 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenoid covalently attached to cysteine residues at or near their C terminus. These proteins constitute up to 2% of total cellular protein in eukaryotic cells. The degradation of prenylated proteins raises a metabolic challenge to the cell, because the thioether bond of the modified cysteine is quite stable. We recently identified and isolated an enzyme termed prenylcysteine lyase that cleaves the prenylcysteine to free cysteine and an isoprenoid product (Zhang, L., Tschantz, W. R., and Casey, P. J. (1997) J. Biol. Chem. 272, 23354-23359). To facilitate the molecular characterization of this enzyme, its cloning was undertaken. Overlapping cDNA clones encoding the complete coding sequence of this enzyme were obtained from a human cDNA library. The open reading frame of the gene encoding prenylcysteine lyase is 1515 base pairs and has a nearly ubiquitous expression pattern with a message size of 6 kilobase pairs. Recombinant prenylcysteine lyase was produced in a baculovirus-Sf9 expression system. Analysis of both the recombinant and native enzyme revealed that the enzyme is glycosylated and contains a signal peptide that is cleaved during processing. Additionally, the subcellular localization of this enzyme was determined to be lysosomal. These findings strengthen the notion that prenylcysteine lyase plays an important role in the final step in the degradation of prenylated proteins and will allow further physiological and biochemical characterization of this enzyme. (+info)
Quorum sensing controls expression of the type III secretion gene transcription and protein secretion in enterohemorrhagic and enteropathogenic Escherichia coli. (8/405)Enterohemorrhagic Escherichia coli O157:H7 and enteropathogenic E. coli cause a characteristic histopathology in intestinal cells known as attaching and effacing. The attaching and effacing lesion is encoded by the Locus of Enterocyte Effacement (LEE) pathogenicity island, which encodes a type III secretion system, the intimin intestinal colonization factor, and the translocated intimin receptor protein that is translocated from the bacterium to the host epithelial cells. Using lacZ reporter gene fusions, we show that expression of the LEE operons encoding the type III secretion system, translocated intimin receptor, and intimin is regulated by quorum sensing in both enterohemorrhagic E. coli and enteropathogenic E. coli. The luxS gene recently shown to be responsible for production of autoinducer in the Vibrio harveyi and E. coli quorum-sensing systems is responsible for regulation of the LEE operons, as shown by the mutation and complementation of the luxS gene. Regulation of intestinal colonization factors by quorum sensing could play an important role in the pathogenesis of disease caused by these organisms. These results suggest that intestinal colonization by E. coli O157:H7, which has an unusually low infectious dose, could be induced by quorum sensing of signals produced by nonpathogenic E. coli of the normal intestinal flora. (+info)
Carbon Monoxide Poisoning Symptoms
The symptoms of carbon monoxide poisoning can vary depending on the level and duration of exposure, but they typically include:
* Dizziness or nausea
* Slurred speech
* Loss of consciousness
In severe cases, carbon monoxide poisoning can cause brain damage, coma, and even death.
Carbon Monoxide Poisoning Causes
Carbon monoxide is a byproduct of incomplete combustion of fuels such as gasoline, natural gas, or wood. Sources of carbon monoxide poisoning include:
* Faulty heating systems or water heaters
* Poorly vented appliances like stoves and fireplaces
* Clogged chimneys or vents
* Running cars in enclosed spaces like garages
* Overcrowding with too many people in a small, poorly ventilated space
Diagnosis of Carbon Monoxide Poisoning
Doctors may suspect carbon monoxide poisoning based on symptoms and medical history. Blood tests can measure the level of carboxyhemoglobin (COHb) in red blood cells, which indicates CO exposure. Chest X-rays or CT scans may also be used to check for signs of lung damage.
Treatment of Carbon Monoxide Poisoning
The treatment of carbon monoxide poisoning involves moving the patient to a location with fresh air and administering oxygen therapy to help remove CO from the bloodstream. In severe cases, medication may be given to help stimulate breathing and improve oxygenation of tissues. Hyperbaric oxygen therapy may also be used in some cases.
Prevention of Carbon Monoxide Poisoning
Prevention is key when it comes to carbon monoxide poisoning. Some steps you can take to prevent CO poisoning include:
* Installing a carbon monoxide detector in your home
* Regularly inspecting and maintaining appliances like furnaces, water heaters, and chimneys
* Properly venting appliances and ensuring they are installed in well-ventilated areas
* Not running cars or generators in enclosed spaces
* Avoiding overcrowding and ensuring there is adequate ventilation in living spaces
Carbon monoxide poisoning is a serious condition that can be fatal if not treated promptly. It's important to be aware of the sources of CO exposure and take steps to prevent it, such as installing carbon monoxide detectors and regularly maintaining appliances. If you suspect CO poisoning, seek medical attention immediately.
The symptoms of carbon tetrachloride poisoning can vary depending on the level and duration of exposure, but may include:
* Respiratory problems, such as coughing, wheezing, and shortness of breath
* Nausea and vomiting
* Abdominal pain and diarrhea
* Headaches and dizziness
* Confusion and disorientation
* Slurred speech and loss of coordination
* Seizures and coma
If you suspect that you or someone else has been exposed to carbon tetrachloride, it is essential to seek medical attention immediately. Treatment for carbon tetrachloride poisoning typically involves supportive care, such as oxygen therapy and hydration, as well as medications to manage symptoms and remove the toxin from the body. In severe cases, hospitalization may be necessary.
Prevention is key when it comes to carbon tetrachloride poisoning. If you work with or are exposed to CTC, it is important to take safety precautions such as wearing protective clothing and equipment, using proper ventilation, and following all safety protocols. It is also essential to handle the chemical with care and store it in a safe location.
In conclusion, carbon tetrachloride poisoning can be a serious and potentially deadly condition that requires immediate medical attention. If you suspect exposure to CTC, it is crucial to seek medical help right away. By taking safety precautions and being aware of the risks associated with this chemical, you can prevent carbon tetrachloride poisoning and protect your health.
1. Poor oral hygiene: When individuals fail to brush and floss regularly, bacteria can accumulate on the teeth, tongue, and gums, leading to bad breath.
2. Gum disease and other oral infections: Gingivitis, periodontitis, and other oral infections can cause bad breath due to the buildup of bacteria and tartar.
3. Dry mouth (xerostomia): A lack of saliva can lead to an increase in bacteria growth and bad breath.
4. Food particles: Eating certain foods, such as garlic or onions, can cause bad breath due to the lingering presence of particles in the mouth.
5. Smoking and tobacco use: Smoking and using other forms of tobacco can lead to bad breath due to the chemicals present in tobacco products.
6. Medical conditions: Certain medical conditions, such as sinus infections, bronchitis, and pneumonia, can cause bad breath.
7. Diet: Consuming certain foods or drinks, such as coffee, tea, or alcohol, can cause bad breath due to their acidic properties.
8. Hormonal changes: Hormonal fluctuations during pregnancy, menstruation, or menopause can lead to changes in the mouth's ecosystem and contribute to bad breath.
9. Dental appliances: Poorly fitting dentures, braces, or other dental appliances can contribute to bad breath.
10. Medications: Certain medications, such as antidepressants and antihistamines, can cause dry mouth and lead to bad breath.
Treatment for halitosis depends on the underlying cause and may include improved oral hygiene, antibiotics, mouthwashes, or other therapies. It is essential to consult a healthcare professional for an accurate diagnosis and appropriate treatment.
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List of EC numbers (EC 3)
Cystathionine beta synthase
List of enzymes
Biological functions of hydrogen sulfide
List of MeSH codes (D08)
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- Ammonia and CO oxidation pathways are enriched in the free-living microbial communities and dissimilatory nitrate reduction to ammonium and H 2 oxidation pathways in the particle-attached, while the Calvin Benson-Bassham cycle is the most prevalent inorganic carbon fixation pathway in both size fractions. (nature.com)
- The primary method of analyzing for sulfur mustard exposure is by detecting the presence of its hydrolysis metabolites in biological fluids. (cdc.gov)
- The purpose of this chapter is to describe the analytical methods that are available for detecting, measuring, and/or monitoring sulfur mustard, its metabolites, and other biomarkers of exposure and effect to sulfur mustard. (cdc.gov)
- The most common currently used method of analyzing for the presence of sulfur mustard and its metabolites in biological and environmental samples is gas chromatography/mass spectrometry (GC/MS). Prior to 1987, however, thin-layer chromatography (TLC) with a colorimetric detection system and gas chromatography with either flame ionization detector (FID), electron capture detector (ECD), or flame photometric detector (FPD) were the most frequently used methods. (cdc.gov)
- Sodium chloride is sometimes added to improve sample stability and prevent sulfur mustard breakdown to thiodiglycol and other metabolites. (cdc.gov)
- Table 7-1 summarizes several representative analytical methods for detecting sulfur mustard and its metabolites in biological samples. (cdc.gov)
- Little information was found on the direct detection of sulfur mustard in biological tissues or fluids. (cdc.gov)
- However, in two cases of suspected exposure, sodium chloride was first added to the urine samples to stabilize any sulfur mustard that might be present. (cdc.gov)
- A semi-quantitative analysis by GC/MS detected low ppb levels of sulfur mustard in these samples compared to none detected in a control sample of a definitely unexposed person (Vycudilik 1985, 1987). (cdc.gov)
- Sulfur mustard has also been detected in body tissues and fluids of an alleged victim (Drasch et al. (cdc.gov)
- 1987). In this analysis, abdominal fat samples were first qualitatively analyzed by GC/MS. Sulfur mustard is generally metabolized rapidly in biological systems. (cdc.gov)
- 7. Carbon monoxide sensitizes cisplatin-resistant ovarian cancer cell lines toward cisplatin via attenuation of levels of glutathione and nuclear metallothionein. (nih.gov)
- The finding that beta-lyase activity exhibited a 2-fold higher Vmax/Km ratio in PT cells than in DT cells, the greater inhibition of both beta-lyase activity and DCVC toxicity by AOAA in PT cells than in DT cells and the lower (40%) S-oxidase activity in PT cells than in DT cells provide evidence for the importance of the beta-lyase in DCVC toxicity in PT cells. (nih.gov)
- temperature exposure [Term] id: XCO:0000012 name: air carbon dioxide content def: "A condition in which the level of carbon dioxide in the air surrounding the organism or breathed by the organism is controlled as part of the experiment. (mcw.edu)
- 10. Erastin sensitizes glioblastoma cells to temozolomide by restraining xCT and cystathionine-γ-lyase function. (nih.gov)
- 17. Reduced Production of Hydrogen Sulfide and Sulfane Sulfur Due to Low Cystathionine β-Synthase Levels in Brain Astrocytes of Stroke-Prone Spontaneously Hypertensive Rats. (nih.gov)
- Addition takes place at the SULFUR . (lookformedical.com)
- Because DCVC was generally more toxic in PT cells and DCVCO was more toxic in DT cells, an attempt was made to correlate in vitro cytotoxicity with the cellular distribution of the beta-lyase and S-oxidase. (nih.gov)
- Three NifS-like proteins, IscS, CSD, and CsdB, from Escherichia coli catalyze the removal of sulfur and selenium from L-cysteine and L-selenocysteine, respectively, to form L-alanine. (nih.gov)
- The lack of IscS also caused a significant loss of the selenium-containing polypeptide of formate dehydrogenase H. Together, these results suggest a dual function of IscS in sulfur and selenium metabolism. (nih.gov)
- We demonstrated using phylogenetics, biochemistry and structural biology that this cysteine-thiol lyase (C-T lyase) is a PLP-dependent enzyme that moved horizontally into a unique monophyletic group of odour-forming staphylococci about 60 million years ago, and has subsequently tailored its enzymatic function to human-derived thioalcohol precursors. (nih.gov)
- 9. Erastin sensitizes glioblastoma cells to temozolomide by restraining xCT and cystathionine-γ-lyase function. (nih.gov)
- With 2 mM S-(2-benzothiazolyl)-L-cysteine as the substrate, approximately two-thirds of the total beta-lyase activity was present in the cytosolic fraction. (nih.gov)
- Cysteine conjugate beta-lyase activity from rat kidney cortex was found in the cystosolic and mitochondrial fractions. (nih.gov)