Clostridium sticklandii
Clostridium
Amino Acid Oxidoreductases
Cobamides
Selenium
Clostridium difficile
Clostridium botulinum
Peptostreptococcus
Pyrroline Carboxylate Reductases
Enterocolitis, Pseudomembranous
Coexpression, purification and characterization of the E and S subunits of coenzyme B(12) and B(6) dependent Clostridium sticklandii D-ornithine aminomutase in Escherichia coli. (1/6)
D-Ornithine aminomutase from Clostridium sticklandii comprises two strongly associating subunits, OraS and OraE, with molecular masses of 12,800 and 82,900 Da. Previous studies have shown that in Escherichia coli the recombinant OraS protein is synthesized in the soluble form and OraE as inclusion bodies. Refolding experiments also indicate that the interactions between OraS and OraE and the binding of either pyridoxal phosphate (PLP) or adenosylcobalamin (AdoCbl) play important roles in the refolding process. In this study, the DNA fragment containing both genes was cloned into the same expression vector and coexpression of the oraE and oraS genes was carried out in E. coli. The solubility of the coexpressed OraS and OraE increases with decreasing isopropyl thio-beta-D-galactoside induction temperature. Among substrate analogues tested, only 2,4-diamino-n-butyric acid displays competitive inhibition of the enzyme with a K(i) of 96 +/- 14 microm. Lys629 is responsible for the binding of PLP. The apparent K(d) for coenzyme B(6) binding to d-ornithine aminomutase is 224 +/- 41 nm as measured by equilibrium dialysis. The mutant protein, OraSE-K629M, is successfully expressed. It is catalytically inactive and unable to bind PLP. Because no coenzyme is involved in protein folding during in vivo translation of OraSE-K629M in E. coli, in vitro refolding of the enzyme employs a different folding mechanism. In both cases, the association of the S and E subunit is important for D-ornithine aminomutase to maintain an active conformation. (+info)A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. (2/6)
Lysine 5,6-aminomutase is an adenosylcobalamin and pyridoxal-5'-phosphate-dependent enzyme that catalyzes a 1,2 rearrangement of the terminal amino group of dl-lysine and of l-beta-lysine. We have solved the x-ray structure of a substrate-free form of lysine-5,6-aminomutase from Clostridium sticklandii. In this structure, a Rossmann domain covalently binds pyridoxal-5'-phosphate by means of lysine 144 and positions it into the putative active site of a neighboring triosephosphate isomerase barrel domain, while simultaneously positioning the other cofactor, adenosylcobalamin, approximately 25 A from the active site. In this mode of pyridoxal-5'-phosphate binding, the cofactor acts as an anchor, tethering the separate polypeptide chain of the Rossmann domain to the triosephosphate isomerase barrel domain. Upon substrate binding and transaldimination of the lysine-144 linkage, the Rossmann domain would be free to rotate and bring adenosylcobalamin, pyridoxal-5'-phosphate, and substrate into proximity. Thus, the structure embodies a locking mechanism to keep the adenosylcobalamin out of the active site and prevent radical generation in the absence of substrate. (+info)The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase. (3/6)
Bacterial prolyl-tRNA synthetases and some smaller paralogs, YbaK and ProX, can hydrolyze misacylated Cys-tRNA Pro or Ala-tRNA Pro. To assess the significance of this quality control editing reaction in vivo, we tested Escherichia coli ybaK for its ability to suppress the E. coli thymidylate synthase thyA:146CCA missense mutant strain, which requires Cys-tRNA(Pro) for growth in the absence of thymine. Missense suppression was observed in a ybaK deletion background, suggesting that YbaK functions as a Cys-tRNA Pro deacylase in vivo. In vitro studies with the full set of 20 E. coli aminoacyl-tRNAs revealed that the Haemophilus influenzae and E. coli YbaK proteins are moderately general aminoacyl-tRNA deacylases that preferentially hydrolyze Cys-tRNA Pro and Cys-tRNA Cys and are also weak deacylases that cleave Gly-tRNA, Ala-tRNA, Ser-tRNA, Pro-tRNA, and Met-tRNA. The ProX protein acted as an aminoacyl-tRNA deacylase that cleaves preferentially Ala-tRNA and Gly-tRNA. The potential of H. influenzae YbaK to hydrolyze in vivo correctly charged Cys-tRNA Cys was tested in E. coli strain X2913 (ybaK+). Overexpression of H. influenzae ybaK decreased the in vivo ratio of Cys-tRNA Cys to tRNA Cys from 65 to 35% and reduced the growth rate of strain X2913 by 30% in LB medium. These data suggest that YbaK-mediated hydrolysis of aminoacyl-tRNA can influence cell growth. (+info)Mechanism of radical-based catalysis in the reaction catalyzed by adenosylcobalamin-dependent ornithine 4,5-aminomutase. (4/6)
(+info)Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase. (5/6)
(+info)Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence. (6/6)
(+info)Amino acid oxidoreductases are a group of enzymes that catalyze the oxidation of amino acids to produce various intermediates, including ammonia, carbon dioxide, and aldehydes or ketones. These enzymes play important roles in various metabolic pathways, including the catabolism of amino acids for energy production and the synthesis of other biomolecules. There are several types of amino acid oxidoreductases, including flavin-dependent enzymes, copper-containing enzymes, and iron-containing enzymes. Some examples of amino acid oxidoreductases include alanine aminotransferase, glutamate dehydrogenase, and ornithine transcarbamylase. In the medical field, amino acid oxidoreductases are often studied in the context of various diseases and disorders, such as liver disease, muscle wasting, and neurodegenerative diseases. Abnormalities in the activity or expression of these enzymes have been implicated in the pathogenesis of these conditions, and targeted therapies based on modulating the activity of amino acid oxidoreductases are being explored as potential treatments.
Cobamides are a class of B vitamins that are essential for the proper functioning of the human body. They are also known as vitamin B12 or cobalamin. Cobamides play a crucial role in the metabolism of fats, carbohydrates, and proteins, as well as in the production of red blood cells and the maintenance of the nervous system. Deficiency in cobamides can lead to a range of health problems, including anemia, neurological disorders, and cognitive impairment. In the medical field, cobamides are often prescribed to treat vitamin B12 deficiency and related conditions.
Ornithine is an amino acid that is naturally present in the body and is involved in various metabolic processes. In the medical field, ornithine is sometimes used as a dietary supplement or medication to treat certain conditions. One of the primary functions of ornithine is to help the body produce the amino acid arginine, which is important for the production of nitric oxide, a molecule that helps to relax blood vessels and improve blood flow. Ornithine has also been studied for its potential to improve athletic performance, reduce muscle soreness, and enhance recovery after exercise. In addition, ornithine has been used to treat a variety of medical conditions, including liver disease, kidney disease, and metabolic disorders such as hyperammonemia, a condition in which there is an excess of ammonia in the blood. It has also been studied for its potential to treat certain types of cancer, although more research is needed to confirm its effectiveness. However, it is important to note that the use of ornithine as a supplement or medication should only be done under the guidance of a healthcare professional, as it can interact with other medications and may have side effects in some people.
Selenium is a trace element that is essential for human health. It is a component of several enzymes that play important roles in the body, including those involved in antioxidant defense, thyroid hormone metabolism, and DNA synthesis. Selenium is also thought to have potential health benefits in preventing certain diseases, such as cancer and cardiovascular disease. In the medical field, selenium is used as a dietary supplement to help prevent and treat selenium deficiency, which can lead to a range of health problems, including fatigue, muscle weakness, and skin problems. Selenium is also used in some cancer treatments, as it has been shown to have anti-cancer properties and may help to reduce the side effects of chemotherapy. However, it is important to note that selenium is toxic in high doses, and excessive intake can lead to health problems such as nausea, vomiting, diarrhea, and hair loss. Therefore, it is important to follow recommended dosages and to speak with a healthcare provider before taking selenium supplements.
Clostridium infections are a group of bacterial infections caused by the genus Clostridium. These bacteria are commonly found in soil, water, and the gastrointestinal tracts of animals and humans. They can cause a variety of infections, including gas gangrene, botulism, and tetanus. Gas gangrene is a serious infection that occurs when Clostridium bacteria release toxins that damage tissue and cause it to die. This can lead to the formation of gas bubbles in the affected tissue, which can cause severe pain and swelling. Botulism is a type of food poisoning caused by a toxin produced by Clostridium botulinum. Tetanus is a serious infection that occurs when Clostridium tetani bacteria release a toxin that affects the nervous system. Clostridium infections can be treated with antibiotics, antitoxins, and supportive care. In some cases, surgery may be necessary to remove infected tissue or repair damage caused by the infection. It is important to seek medical attention promptly if you suspect that you or someone else may have a Clostridium infection, as prompt treatment is essential for a good outcome.
Pyrroline carboxylate reductases (PYCRs) are a family of enzymes that play a role in the metabolism of proline and other amino acids. In the medical field, PYCRs have been implicated in a number of diseases, including cancer, neurodegenerative disorders, and metabolic disorders such as diabetes. PYCRs are involved in the conversion of pyrroline-5-carboxylate (P5C) to glutamate semialdehyde (GSA), a key step in the biosynthesis of proline. P5C is a toxic compound that is produced as a byproduct of the metabolism of proline and other amino acids. PYCRs help to detoxify P5C by converting it to GSA, which can then be further metabolized to proline or other amino acids. In cancer, PYCRs have been shown to play a role in the development and progression of the disease. For example, high levels of PYCR1 have been associated with poor prognosis in patients with breast cancer and lung cancer. PYCR1 has also been shown to promote the growth and survival of cancer cells by regulating the metabolism of proline and other amino acids. In neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, PYCRs have been implicated in the accumulation of toxic protein aggregates that are characteristic of these diseases. PYCRs have been shown to regulate the metabolism of proline and other amino acids, which can affect the stability and aggregation of proteins. In metabolic disorders such as diabetes, PYCRs have been shown to play a role in the regulation of glucose metabolism. PYCRs have been shown to regulate the levels of proline and other amino acids, which can affect the metabolism of glucose and other nutrients. Overall, PYCRs are a family of enzymes that play a important role in the metabolism of proline and other amino acids. In the medical field, PYCRs have been implicated in a number of diseases, including cancer, neurodegenerative disorders, and metabolic disorders such as diabetes.
Enterocolitis, pseudomembranous, also known as Clostridium difficile colitis, is an inflammatory condition of the colon that is caused by the overgrowth of the bacterium Clostridium difficile. This bacterium is normally present in the gut in small numbers, but when the balance of bacteria in the gut is disrupted, it can overgrow and produce toxins that damage the colon. The symptoms of pseudomembranous enterocolitis can include diarrhea, abdominal pain, fever, and nausea. In severe cases, the condition can lead to dehydration, electrolyte imbalances, and even death. Pseudomembranous enterocolitis is typically treated with antibiotics to target the overgrowth of C. difficile and the toxins it produces. In some cases, hospitalization may be necessary to manage symptoms and prevent complications.
Acetoanaerobium sticklandii
Leland S. McClung
2,4-diaminopentanoate dehydrogenase
List of Clostridium species
Ornithine racemase
Beta-lysine 5,6-aminomutase
Proline racemase
Clostridium aminophilum
D-proline reductase (dithiol)
D-lysine 5,6-aminomutase
Betaine reductase
Glycine reductase
List of MeSH codes (B03)
Toxins | Free Full-Text | Rumen and Serum Metabolomes in Response to Endophyte-Infected Tall Fescue Seed and Isoflavone...
Pre GI: BLASTP Hits
Clusters of Characterized Proteins
SCOPe 2.08: Protein: D-lysine 5,6-aminomutase beta subunit KamE, C-terminal domain
Global transcriptional control by glucose and
Species: Clostridium caldaquaticum
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Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence -...
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Discoveries of vitamin B12 and selenium enzymes - PubMed
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Code System Concept
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NEW (2005) MESH HEADINGS WITH SCOPE NOTES (UNIT RECORD FORMAT; 8/13/2004
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NATIONAL INSTITUTES OF HEALTH
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TERM
Difficile1
- By whole transcriptome analyses, we characterized glucosedependent and CcpA-dependent gene regulation in Clostridium difficile. (studyres.com)
Bacteria2
- Especie tipo del género CLOSTRIDIUM, bacteria grampositiva de la familia Clostridiaceae. (bvsalud.org)
- Type species of the genus CLOSTRIDIUM, a gram-positive bacteria in the family Clostridiaceae. (bvsalud.org)