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Oxidases
In biochemistry, an oxidase is an oxidoreductase (any enzyme that catalyzes a redox reaction) that uses 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. The use of dioxygen is the only unifying feature; in the EC classification, these enzymes are scattered in many categories. Examples An important example is EC 7.1.1.9 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: * EC 1.1.3.4 Glucose oxidase * EC 1.4.3.4 Monoamine oxidase * EC 1.14.-.- Cytochrome P450 oxidase * EC 1.6.3.1 NADPH oxidase * EC 1.17.3.2 Xanthine oxidase * EC 1.1.3.8 L-gulonolactone oxidase * EC 1.10 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Transfer Chain
An electron transport chain (ETC) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. Many of the enzymes in the electron transport chain are embedded within the membrane. The flow of electrons through the electron transport chain is an exergonic process. The energy from the redox reactions creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP). In aerobic respiration, the flow of electrons terminates with molecular oxygen as the final electron acceptor. In anaerobic respiration, other electron acceptors are used, such as sulfate. In an electron transport chain, the redox reactions are driven by the difference in the Gibbs free energy of reactants and products. The free energy released when a higher ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyphenol Oxidase
Polyphenol oxidase (PPO; also polyphenol oxidase i, chloroplastic), an enzyme involved in fruit browning, is a tetramer that contains four atoms of copper per molecule. PPO may accept monophenols and/or ''o''-diphenols as substrates. The enzyme works by catalyzing the ''o''- hydroxylation of monophenol molecules in which the benzene ring contains a single hydroxyl substituent to ''o''-diphenols (phenol molecules containing two hydroxyl substituents at the 1, 2 positions, with no carbon between). It can also further catalyse the oxidation of ''o''-diphenols to produce ''o''-quinones. PPO catalyses the rapid polymerization of ''o''-quinones to produce black, brown or red pigments (polyphenols) that cause fruit browning. The amino acid tyrosine contains a single phenolic ring that may be oxidised by the action of PPOs to form ''o''-quinone. Hence, PPOs may also be referred to as tyrosinases. Common foods producing the enzyme include mushrooms ('' Agaricus bisporus ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monoamine Oxidase
Monoamine oxidases (MAO) () are a family of enzymes that catalyze the oxidation of monoamines, employing oxygen to clip off their amine group. They are found bound to the outer membrane of mitochondria in most cell types of the body. The first such enzyme was discovered in 1928 by Mary Bernheim in the liver and was named tyramine oxidase. The MAOs belong to the protein family of flavin-containing amine oxidoreductases. MAOs are important in the breakdown of monoamines ingested in food, and also serve to inactivate monoamine neurotransmitters. Because of the latter, they are involved in a number of psychiatric and neurological diseases, some of which can be treated with monoamine oxidase inhibitors (MAOIs) which block the action of MAOs. Subtypes and tissue distribution In humans there are two types of MAO: MAO-A and MAO-B. * Both are found in neurons and astroglia. * Outside the central nervous system: ** MAO-A is also found in the liver, pulmonary vascular end ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NADPH Oxidase
NADPH oxidase (nicotinamide adenine dinucleotide phosphate oxidase) is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms. Human Protein isoform, isoforms of the catalytic component of the complex include NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Reaction NADPH oxidase catalyzes the production of a superoxide free radical by transferring one electron to oxygen from NADPH. : Types In mammals, NADPH oxidase is found in two types: one in white blood cells (neutrophilic) and the other in Blood vessel, vascular cells, differing in biochemical structure and functions. Neutrophilic NADPH oxidase produces superoxide almost instantaneously, whereas the vascular enzyme produces superoxide in minutes to hours. Moreover, in white blood cells, superoxide has been found to transfer electrons across the membrane to extracellula ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lysyl Oxidase
Lysyl oxidase (LOX), also known as protein-lysine 6-oxidase, is an enzyme that, in humans, is encoded by the ''LOX'' gene. It catalyzes the conversion of lysine residues into its aldehyde derivative allysine. Allysine form cross-links in extracellular matrix proteins. Inhibition of lysyl oxidase can cause osteolathyrism, but, at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous. Structure In the yeast species ''Pichia pastoris'', lysyl oxidase constitutes a homodimeric structure. Each monomer consists of an active site that includes a Cu(II) atom, coordinated by three histidine residues, as well as 2,4,5-trihydroxyphenylalanine quinone (TPQ), a crucial cofactor. In humans, the LOX gene is located on chromosome 5 q23.3-31.2. The DNA sequence encodes a polypeptide of 417 amino acids, the first 21 residues of which constitute a signal peptide, with a weight of approximately 32 kDa. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
L-gulonolactone Oxidase
L-Gulonolactone oxidase ( ECbr>1.1.3.8 is an enzyme that produces vitamin C. It is expressed in most mammals, but is non-functional in Haplorrhini (a suborder of primates, including humans), in some bats, and in guinea pigs. It catalyzes the reaction of L-gulono-1,4-lactone with oxygen to form L-xylo-hex-3-gulonolactone (2-keto-gulono-γ-lactone) and hydrogen peroxide. It uses FAD as a cofactor. The L-xylo-hex-3-gulonolactone then converts to ascorbic acid spontaneously, without enzymatic action. The structure of L-gulonolactone oxidase in rats helps identify characteristics of this enzyme. Gulonolactone oxidase deficiency The non-functional gulonolactone oxidase pseudogene (''GULOP'') was mapped to human chromosome 8p21, which corresponds to an evolutionarily conserved segment on either porcine chromosome 4 (SSC4) or 14 (SSC14). GULO produces the precursor to ascorbic acid, which spontaneously converts to the vitamin itself. The loss of activity of the gene encoding L-gul ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydrogen Peroxide
Hydrogen peroxide is a chemical compound with the formula . In its pure form, it is a very pale blue liquid that is slightly more viscosity, viscous than Properties of water, water. It is used as an oxidizer, bleaching agent, and antiseptic, usually as a dilute solution (3%–6% by weight) in water for consumer use and in higher concentrations for industrial use. Concentrated hydrogen peroxide, or "high-test peroxide", decomposes explosively when heated and has been used as both a monopropellant and an oxidizer in rocketry. Hydrogen peroxide is a reactive oxygen species and the simplest peroxide, a compound having an oxygen–oxygen single bond. It decomposes slowly into water and elemental oxygen when exposed to light, and rapidly in the presence of organic or reactive compounds. It is typically stored with a Stabilizer (chemistry), stabilizer in a weakly acidic solution in an opaque bottle. Hydrogen peroxide is found in biological systems including the human body. Enzymes that u ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Thiol
In organic chemistry, a thiol (; ), or thiol derivative, is any organosulfur compound of the form , where R represents an alkyl or other organic substituent. The functional group itself is referred to as either a thiol group or a sulfhydryl group, or a sulfanyl group. Thiols are the sulfur analogue of alcohols (that is, sulfur takes the place of oxygen in the hydroxyl () group of an alcohol), and the word is a blend of "''thio-''" with "alcohol". Many thiols have strong odors resembling that of garlic, cabbage or rotten eggs. Thiols are used as odorants to assist in the detection of natural gas (which in pure form is odorless), and the smell of natural gas is due to the smell of the thiol used as the odorant. Nomenclature Thiols are sometimes referred to as mercaptans () or mercapto compounds, a term introduced in 1832 by William Christopher Zeise and is derived from the Latin ('capturing mercury')''Oxford American Dictionaries'' (Mac OS X Leopard). because the thiolate grou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Microbiology
Microbiology () is the branches of science, scientific study of microorganisms, those being of unicellular organism, unicellular (single-celled), multicellular organism, multicellular (consisting of complex cells), or non-cellular life, acellular (lacking cells). Microbiology encompasses numerous sub-disciplines including virology, bacteriology, protistology, mycology, immunology, and parasitology. The organisms that constitute the microbial world are characterized as either prokaryotes or eukaryotes; eukaryote, Eukaryotic microorganisms possess membrane-bound organelles and include fungi and protists, whereas prokaryote, prokaryotic organisms are conventionally classified as lacking membrane-bound organelles and include Bacteria and Archaea. Microbiologists traditionally relied on culture, staining, and microscopy for the isolation and identification of microorganisms. However, less than 1% of the microorganisms present in common environments can be cultured in isolation using c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxidase Test
The oxidase test is used to determine whether an organism possesses the cytochrome c oxidase enzyme. The test is used as an aid for the differentiation of ''Neisseria'', ''Moraxella'', ''Campylobacter'' and ''Pasteurella'' species (oxidase positive). It is also used to differentiate pseudomonads from related species.MacFaddin JF, editor. Biochemical Tests for Identification of Medical Bacteria. 3rd ed. Philadelphia:Lippincott Williams and Wilkins; 2000. p. 363-7 Classification Strains may be either oxidase-positive (OX+) or oxidase-negative (OX-). OX+ OX+ normally means the bacterium contains cytochrome c oxidase (also known as Complex IV) and can therefore use oxygen for energy production by converting O2 to H2O2 or H2O with an electron transfer chain. The Pseudomonadaceae are typically OX+. The Gram-negative diplococci Neisseria and Moraxella are oxidase-positive. Many Gram-negative, spiral curved rods are also oxidase-positive, which includes ''Helicobacter pylori'', ''Vibrio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sulfhydryl Oxidase
In enzymology, a thiol oxidase () is an enzyme that catalysis, catalyzes the chemical reaction :4 R'C(R)SH + O2 \rightleftharpoons 2 R'C(R)S-S(R)CR' + 2 H2O Thus, the two substrate (biochemistry), substrates of this enzyme are R'C(R)SH and oxygen, O2, whereas its two product (chemistry), products are R'C(R)S-S(R)CR' and water, H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The List of enzymes, systematic name of this enzyme class is thiol:oxygen oxidoreductase. This enzyme is also called sulfhydryl oxidase. References * * EC 1.8.3 Enzymes of unknown structure {{1.8-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
