|
Pasteurella Canis
''Pasteurella canis'' is a Gram-negative, nonmotile, penicillin-sensitive coccobacillus of the family Pasteurellaceae. Bacteria from this family cause zoonotic infections in humans, which manifest themselves as skin or soft-tissue infections after an animal bite. It has been known to cause serious disease in immunocompromised patients. ''Pasteurella'' was first described around 1880 and thought to be associated with chicken cholera and hemorrhagic septicemia in animals. The genus was first cultured in 1885. In 1920, strains of ''Pasteurella'' were isolated and observed in human infections. Nomenclature “''Micrococcus gallicidus''” was the first scientific name used for these bacteria. For a short time, the bacteria were unofficially placed in different genera, such as ''Octopsis'', ''Coccobacillus'', and ''Eucystia''. In 1887, genus “''Pasteurella''” was proposed to honor Louis Pasteur for his critical discoveries in the field of microbiology. Before molecular tech ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gram-negative
Gram-negative bacteria are bacteria that do not retain the crystal violet stain used in the Gram staining method of bacterial differentiation. They are characterized by their cell envelopes, which are composed of a thin peptidoglycan cell wall sandwiched between an inner cytoplasmic cell membrane and a bacterial outer membrane. Gram-negative bacteria are found in virtually all environments on Earth that support life. The gram-negative bacteria include the model organism ''Escherichia coli'', as well as many pathogenic bacteria, such as ''Pseudomonas aeruginosa'', ''Chlamydia trachomatis'', and ''Yersinia pestis''. They are a significant medical challenge as their outer membrane protects them from many antibiotics (including penicillin), detergents that would normally damage the inner cell membrane, and lysozyme, an antimicrobial enzyme produced by animals that forms part of the innate immune system. Additionally, the outer leaflet of this membrane comprises a complex lipo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Facultative Anaerobic
A facultative anaerobic organism is an organism that makes ATP by aerobic respiration if oxygen is present, but is capable of switching to fermentation if oxygen is absent. Some examples of facultatively anaerobic bacteria are '' Staphylococcus'' spp., ''Escherichia coli'', '' Salmonella'', ''Listeria'' spp., ''Shewanella oneidensis'' and ''Yersinia pestis''. Certain eukaryotes are also facultative anaerobes, including fungi such as ''Saccharomyces cerevisiae'' and many aquatic invertebrates such as nereid polychaetes. See also * Aerobic respiration * Anaerobic respiration * Fermentation * Obligate aerobe * Obligate anaerobe * Microaerophile A microaerophile is a microorganism that requires environments containing lower levels of dioxygen than that are present in the atmosphere (i.e. < 21% O2; typically 2–10% O2) for optimal growth. A more re ... References External links |
Arabinose
Arabinose is an aldopentose – a monosaccharide containing five carbon atoms, and including an aldehyde (CHO) functional group. For biosynthetic reasons, most saccharides are almost always more abundant in nature as the "D"-form, or structurally analogous to D-glyceraldehyde.The D/L nomenclature does not refer to the molecule's optical rotation properties but to its structural analogy to glyceraldehyde. However, L-arabinose is in fact more common than D-arabinose in nature and is found in nature as a component of biopolymers such as hemicellulose and pectin. The L-arabinose operon, also known as the araBAD operon, has been the subject of much biomolecular research. The operon directs the catabolism of arabinose in ''E. coli'', and it is dynamically activated in the presence of arabinose and the absence of glucose. A classic method for the organic synthesis of arabinose from glucose is the Wohl degradation. : Etymology Arabinose gets its name from gum arabic, from which i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Maltose
} Maltose ( or ), also known as maltobiose or malt sugar, is a disaccharide formed from two units of glucose joined with an α(1→4) bond. In the isomer isomaltose, the two glucose molecules are joined with an α(1→6) bond. Maltose is the two-unit member of the amylose homologous series, the key structural motif of starch. When beta-amylase breaks down starch, it removes two glucose units at a time, producing maltose. An example of this reaction is found in germinating seeds, which is why it was named after malt. Unlike sucrose, it is a reducing sugar. History Maltose was discovered by Augustin-Pierre Dubrunfaut, although this discovery was not widely accepted until it was confirmed in 1872 by Irish chemist and brewer Cornelius O'Sullivan. Its name comes from malt, combined with the suffix ' -ose' which is used in names of sugars. Structure and nomenclature Carbohydrates are generally divided into monosaccharides, oligosaccharides, and polysaccharides depending on the nu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Urease
Ureases (), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. Ureases are found in numerous bacteria, fungi, algae, plants, and some invertebrates, as well as in soils, as a soil enzyme. They are nickel-containing metalloenzymes of high molecular weight. These enzymes catalyze the hydrolysis of urea into carbon dioxide and ammonia: : (NH2)2CO + H2O CO2 + 2NH3 The hydrolysis of urea occurs in two stages. In the first stage, ammonia and carbamic acid are produced. The carbamate spontaneously and rapidly hydrolyzes to ammonia and carbonic acid. Urease activity increases the pH of its environment as ammonia is produced, which is basic. History Its activity was first identified in 1876 by Frédéric Alphonse Musculus as a soluble ferment. In 1926, James B. Sumner, showed that urease is a protein by examining its crystallized form. Sumner's work was the first demonstration that a protein can function as an enzyme and led eventually to the reco ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sorbitol
Sorbitol (), less commonly known as glucitol (), is a sugar alcohol with a sweet taste which the human body metabolizes slowly. It can be obtained by reduction of glucose, which changes the converted aldehyde group (−CHO) to a primary alcohol group (−CH2OH). Most sorbitol is made from potato starch, but it is also found in nature, for example in apples, pears, peaches, and prunes. It is converted to fructose by sorbitol-6-phosphate 2-dehydrogenase. Sorbitol is an isomer of mannitol, another sugar alcohol; the two differ only in the orientation of the hydroxyl group on carbon 2.Kearsley, M. W.; Deis, R. C. Sorbitol and Mannitol. In Sweeteners and Sugar Alternatives in Food Technology; Ames: Oxford, 2006; pp 249-249-261. While similar, the two sugar alcohols have very different sources in nature, melting points, and uses. As an over-the-counter drug, sorbitol is used as a laxative to treat constipation. Synthesis Sorbitol may be synthesised via a glucose reduction reaction in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dulcitol
Galactitol (dulcitol) is a sugar alcohol, the reduction product of galactose. It has a slightly sweet taste. In people with galactokinase deficiency, a form of galactosemia, excess dulcitol forms in the lens of the eye leading to cataracts. Galactitol is produced from galactose in a reaction catalyzed by aldose reductase. The other common galactose metabolism defect is a defect in galactose-1-phosphate uridylyltransferase Galactose-1-phosphate uridylyltransferase (or GALT, G1PUT) is an enzyme () responsible for converting ingested galactose to glucose. Galactose-1-phosphate uridylyltransferase (GALT) catalyzes the second step of the Leloir pathway of galactose ..., an autosomal recessive disorder, which also causes a buildup of galactitol as a result of increased concentrations of galactose-1-phosphate and galactose. This disorder leads to cataracts caused by galactitol buildup. References External links * {{Fructose and galactose metabolic intermediates Sugar alc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
D-mannitol
Mannitol is a type of sugar alcohol used as a sweetener and medication. It is used as a low calorie sweetener as it is poorly absorbed by the intestines. As a medication, it is used to decrease pressure in the eyes, as in glaucoma, and to lower increased intracranial pressure. Medically, it is given by injection or inhalation. Effects typically begin within 15 minutes and last up to 8 hours. Common side effects from medical use include electrolyte problems and dehydration. Other serious side effects may include worsening heart failure and kidney problems. It is unclear if use is safe in pregnancy. Mannitol is in the osmotic diuretic family of medications and works by pulling fluid from the brain and eyes. The discovery of mannitol is attributed to Joseph Louis Proust in 1806. It is on the World Health Organization's List of Essential Medicines. It was originally made from the flowering ash and called manna due to its supposed resemblance to the Biblical food. Mannitol is on ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nicotinamide Adenine Dinucleotide
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen), respectively. In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The cofactor is, therefore, found in two forms in cells: NAD is an oxidizing agent – it accepts electrons from other molecules and becomes reduced. This reaction, also with H+, forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD. However, it is also used in other cellular processes, most notably as a substrate of enzymes in adding or removing chemical groups to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lysine Decarboxylase
The enzyme Lysine decarboxylase () converts lysine to cadaverine Cadaverine is an organic compound with the formula (CH2)5(NH2)2. Classified as diamine, it is a colorless liquid with an unpleasant odor. It is present in small quantities in living organisms but is often associated with the putrefaction of anim .... References External links * EC 4.1.1 {{enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ornithine Decarboxylase
The enzyme ornithine decarboxylase (, ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) to form putrescine. This reaction is the committed step in polyamine synthesis. In humans, this protein has 461 amino acids and forms a homodimer. Reaction mechanism Lysine 69 on ornithine decarboxylase (ODC) binds the cofactor pyridoxal phosphate to form a Schiff base. Ornithine displaces the lysine to form a Schiff base attached to orthonine, which decarboxylates to form a quinoid intermediate. This intermediate rearranges to form a Schiff base attached to putrescine, which is attacked by lysine to release putrescine product and reform PLP-bound ODC. This is the first step and the rate-limiting step in humans for the production of polyamines, compounds required for cell division. Structure image:Ornithine Decarboxylase Publication View.png, 270px, 3D crystal structure of ornithine decarboxylase.; ; rendered viPyMOL The active form of ornithine decarboxyla ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxidase
In biochemistry, an oxidase is an enzyme that catalyzes oxidation-reduction reactions, especially one involving dioxygen (O2) as the electron acceptor. In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H2O) or hydrogen peroxide (H2O2). Some oxidation reactions, such as those involving monoamine oxidase or xanthine oxidase, typically do not involve free molecular oxygen. The oxidases are a subclass of the oxidoreductases. Examples An important example is cytochrome c oxidase, the key enzyme that allows the body to employ oxygen in the generation of energy and the final component of the electron transfer chain. Other examples are: * Glucose oxidase * Monoamine oxidase * Cytochrome P450 oxidase * NADPH oxidase * Xanthine oxidase * L-gulonolactone oxidase * Laccase * Lysyl oxidase * Polyphenol oxidase * Sulfhydryl oxidase. This enzyme oxidises thiol groups. Oxidase test In microbiology, the oxidase test is used as a phenotypic characteristic for t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
