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English Wikipedia references for Expasy.org 1-50 of 22992
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| Adenylate cyclase Adenylate cyclase (, also known as adenylyl cyclase, adenyl cyclase or AC) is a lyase enzyme. It is a part of the cAMP dependent pathway Adenylate_cyclase | |
| Beta-lactamase Beta-lactamases are enzymes () produced by some bacteria and are responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins (are relatively resistant to beta-lactamase), cephamycins, and carbapenems (ertapenem). These antibiotics have a common element in their molecular structurebeta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Beta-lactamase | |
| Chymotrypsin Chymotrypsin (bovine γ chymotrypsinproteolysis. Chymotrypsin cleaves peptides at the carboxyl side of tyrosine, tryptophan, and phenylalanine because these three amino acids contain aromatic rings, which fit into a 'hydrophobic pocket' in the enzyme. Over time, chymotrypsin also hydrolyzes other amide bonds, particularly those with leucine-donated carboxyls. Chymotrypsin | |
| Calreticulin Calreticulin is a multifunctional protein that binds Ca2+ ions (a second messenger molecule in signal transduction), rendering it inactive. The Ca2+ is bound with low affinity, but high capacity, and can be released on a signal (see inositol triphosphate). Calreticulin is located in storage compartments associated with the endoplasmic reticulum.Calreticulin is also known as calregulin, CRP55, CaBP3 and calsequestrin-like protein. Calreticulin | |
| DNA ligase In molecular biology, DNA ligase is a special type of ligase () that can link together two DNA strands that have double-strand break (a break in both complementary strands of DNA). The alternative, a single-strand break, is fixed by a different type of DNA ligase using the complementary strand as a template but still requires DNA ligase to create the final phosphodiester bond to fully repair the DNA. DNA_ligase | |
| Enzyme Enzymes are biomolecules that catalyze (i.e., increase the rates of) chemical reactions. Nearly all known enzymes are proteins. However, certain RNA molecules can be effective biocatalysts too. These RNA molecules have come to be known as ribozymes. In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, called the products. Enzyme | |
| Glycolysis Glycolysis (from glycose, an older term for glucose + -lysis degradation) is the metabolic pathway that converts glucose, C6H12O6, into pyruvate, C3H3O3-. The free energy released in this process is used to form the high energy compounds, ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide). Glycolysis | |
| Insulin Insulin is a hormone that has extensive effects on metabolism and other body functions, such as vascular compliance. Insulin causes cells in the liver, muscle, and fat tissue to take up glucose from the blood, storing it as glycogen in the liver and muscle, and stopping use of fat as an energy source. Insulin | |
| Insulin Talk:Insulin | |
| Integrin Integrins are receptors that mediate attachment between a cell and the tissues surrounding it, which may be other cells or the extracellular matrix (ECM). They also play a role in cell signaling and thereby define cellular shape, mobility, and regulate the cell cycle.Typically, receptors inform a cell of the molecules in its environment and the cell evokes a response. Integrin | |
| Lactase Lactase (LCT), a part of the β-galactosidase family of enzymes, is a glycoside hydrolase involved in the hydrolysis of the disaccharide lactose into constituent galactose and glucose monomers. In humans, lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine.Lactase is essential for digestive hydrolysis of lactose in milk. Deficiency of the enzyme causes lactose intolerance. Lactase | |
| Metabolism Metabolism is the set of chemical reactions that occur in living organisms in order to maintain life. These processes allow organisms to grow and reproduce, maintain their structures, and respond to their environments. Metabolism is usually divided into two categories. Catabolism breaks down organic matter, for example to harvest energy in cellular respiration. Anabolism, on the other hand, uses energy to construct components of cells such as proteins and nucleic acids. Metabolism | |
| Monoamine oxidase Monoamine oxidases (singular abbreviation MAO) () are enzymes that catalyze the oxidation of monoamines. They are found bound to the outer membrane of mitochondria in most cell types in the body. The enzyme was discovered by Mary Hare in the liver, and received the name of tyramine oxidase. They belong to protein family of flavin-containing amine oxidoreductases. Monoamine_oxidase | |
| Protein Proteins (also known as polypeptides) are organic compounds made of amino acids arranged in a linear chain. The amino acids in a polymer chain are joined together by the peptide bonds between the carboxyl and amino groups of adjacent amino acid residues. The sequence of amino acids in a protein is defined by the sequence of a gene, which is encoded in the genetic code. Protein | |
| Platypus The Platypus (Ornithorhynchus anatinus) is a semi-aquatic mammal endemic to eastern Australia, including Tasmania. Together with the four species of echidna, it is one of the five extant species of monotremes, the only mammals that lay eggs instead of giving birth to live young. It is the sole living representative of its family (Ornithorhynchidae) and genus (Ornithorhynchus), though a number of related species have been found in the fossil record. Platypus | |
| Protein kinase protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. Protein_kinase | |
| P53 p53 (also known as protein 53 or tumor protein 53), is a transcription factor which in humans is encoded by the TP53 gene. p53 is important in multicellular organisms, where it regulates the cell cycle and thus functions as a tumor suppressor that is involved in preventing cancer. As such, p53 has been described as "the guardian of the genome," "the guardian angel gene," and the "master watchman," referring to its role in conserving stability by preventing genome mutation. P53 | |
| Reverse transcriptase In biochemistry, a reverse transcriptase, also known as RNA-dependent DNA polymerase, is a DNA polymerase enzyme that transcribes single-stranded RNA into single-stranded DNA. It also helps in the formation of a double helix DNA once the RNA has been reverse transcribed into a single strand cDNA. Normal transcription involves the synthesis of RNA from DNA; hence, reverse transcription is the reverse of this. Reverse_transcriptase | |
| Rennet Rennet () is a natural complex of enzymes produced in any mammalian stomach to digest the mother's milk, and is often used in the production of cheese. Rennet contains many enzymes, including a proteolytic enzyme (protease) that coagulates the milk, causing it to separate into solids (curds) and liquid (whey). Rennet | |
| Superoxide dismutase Superoxide dismutases (SOD, ) are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism. Superoxide_dismutase | |
| SH3 domain The SRC HOMOLOGY 3 DOMAIN (or SH3 domain) is a small protein domain of about 60 amino acids residues first identified as a conserved sequence in the viral adaptor protein v-Crk and the non-catalytic parts of enzymes such as phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src. It has also been identified in several other protein families such asPI3 Kinase, Ras GTPase activating protein, CDC24 and CDC25. SH3_domain | |
| Trypsin Trypsin () is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin predominantly cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. Trypsin | |
| Tertiary structure biochemistry and chemistry, the tertiary structure of a protein or any other macromolecule is its three-dimensional structure, as defined by the atomic coordinates. Tertiary_structure | |
| Catalase Catalase is a common enzyme found in nearly all living organisms which are exposed to oxygen, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second.Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. Catalase | |
| Möbius strip This article is about the mathematical object. See Mobius Band (music group) for the music group. Möbius strip or Möbius band ( or in English, in German) (alternatively written Mobius or Moebius in English) is a surface with only one side and only one boundary component. The Möbius strip has the mathematical property of being non-orientable. It is also a ruled surface. It was discovered independently by the German mathematicians August Ferdinand Möbius and Johann Benedict Listing in 1858. Möbius_strip | |
| Chitinase Chitinases are digestive enzymes that break down glycosidic bonds in chitin. Because chitin composes the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are generally found in organisms that either need to reshape their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinase | |
| Tyrosine kinase A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to a tyrosine residue in a protein. Tyrosine kinases are a subgroup of the larger class of protein kinases. Phosphorylation of proteins by kinases is an important mechanism in signal transduction for regulation of enzyme activity. There are over 100 3D structures of tyrosine kinases available at the Protein Data Bank. An example is PDB 1IRK, the crystal structure of the tyrosine kinase domain of the human insulin receptor. Tyrosine_kinase | |
| Folic acid Folic acid (also known as Vitamin B9 or Folacin) and Folate (the naturally occurring form) are forms of the water-soluble Vitamin B9. Vitamin B9 (Folic acid and Folate inclusive) is essential to numerous bodily functions ranging from nucleotide synthesis to the remethylation of homocysteine. Folic_acid | |
| Ebola Ebola is the common term for a group of viruses belonging to genus Ebolavirus (EBOV), which is a part of the family Filoviridae, and for the disease that they cause, Ebolahemorrhagic. The virus is named after the Ebola River, where the first recognized outbreak of Ebola hemorrhagic fever occurred. The viruses are characterized by long filaments, and have a shape similar to that of the Marburg virus, also in the family Filoviridae, and possessing similar disease symptoms. Ebola | |
| Protease This article discusses primarily the structure and properties of proteolytic enzymes. For medical, surgical and related applications of several proteases, see articleProteases (medical and related uses) A protease is any enzyme that conducts proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in the polypeptide chain, which form a molecule of protein. Protease | |
| Adrenocorticotropic hormone Adrenocorticotropic hormone (ACTH or corticotropin) is a polypeptide tropic hormone produced and secreted by the anterior pituitary gland. It is an important component of the hypothalamic-pituitary-adrenal axis and is often produced in response to biological stress (along with corticotropin-releasing hormone from the hypothalamus). Its principal effects are increased production of androgens and, as its name suggests, cortisol from the adrenal cortex. Adrenocorticotropic_hormone | |
| Ebola Talk:Ebola | |
| Marburg virus Marburg virus or simply Marburg is the common name for the the genus of viruses Marburgvirus, which contains one species, Lake Victoria marburgvirus. The virus causes the disease Marburg Hemorrhagic Fever (MHF), also referred to as Marburg Virus Disease. Marburg originated in Central and East Africa, and infects both human and nonhuman primates. The Marburg Virus is in the same taxonomic family as Ebola, and both are identical structurally although produce different antibodies. Marburg_virus | |
| Endorphin Endorphins are endogenous opioid polypeptide compounds. They are produced by the pituitary gland and the hypothalamus in vertebrates during strenuous exercise, excitement, pain, death, and orgasm, and they resemble the opiates in their abilities to produce analgesia and a sense of well-being. Endorphins work as "natural pain relievers", whose effects may be enhanced by other medications. Endorphin | |
| Reelin Reelin is a protein that helps regulate processes of neuronal migration and positioning in the developing brain. Besides this important role in early development, reelin continues to work in the adult brain. It modulates the synaptic plasticity by enhancing the induction and maintenance of long-term potentiation. Reelin | |
| Amylase An amylase is an enzyme that breaks starch down into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. Foods that contain much starch but little sugar, such as rice and potato, taste slightly sweet as they are chewed because amylase turns some of their starch into sugar in the mouth. Amylase | |
| Chymosin Chymosin | |
| Beta-galactosidase β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Alternate or nicknames are "beta-gal" or "β-gal". Lactase is often confused as an alternative name for β-galactosidase, but it is actually simply a sub-class of β-galactosidase. Beta-galactosidase | |
| Flaviviridae The Flaviviridae are a family of viruses that are primarily spread through arthropod vectors (mainly ticks and mosquitoes). The family gets its name from Yellow Fever virus, a type virus of Flaviviridae; flavus means yellow in Latin. (Yellow fever in turn was named because of its propensity to cause jaundice in victims.) Flaviviridae | |
| Glutathione Glutathione (GSH) is a tripeptide. It contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side chain. Glutathione, an antioxidant, protects cells from toxins such as free radicals.Thiol groups are kept in a reduced state at a concentration of approximately ~5 mM in animal cells. Glutathione | |
| SRY SRY (Sex-determining Region Y) is a sex-determining gene on the Y chromosome in the therians (placental mammals and marsupials).This intronless gene encodes a transcription factor that is a member of the high mobility group (HMG)-box family of DNA-binding proteins. SRY | |
| Alcohol dehydrogenase Alcohol dehydrogenases (ADH) () are a group of seven dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of NAD+ to NADHhumans and many other animals, they serve to break down alcohols which could otherwise be toxic; in yeast and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation. Alcohol_dehydrogenase | |
| Myoglobin Myoglobin is a single-chain globular protein of 153 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds. It has eight alpha helices and a hydrophobic core. It has a molecular weight of 16,700 daltons, and is the primary oxygen-carrying pigment of muscle tissues. Myoglobin | |
| Electron transport chain An electron transport chain couples a chemical reaction between an electron donor (such as NADH) and an electron acceptor (such as O2) to the transfer of H+ ions across a membrane, through a set of mediating biochemical reactions. These H+ ions are used to produce adenosine triphosphate (ATP), the main energy intermediate in living organisms, as they move back across the membrane. Electron transport chains are used for extracting energy from sunlight Electron_transport_chain | |
| Cytochrome c Cytochrome c, or cyt c (horse heartPDB 1HRC) is a small haem protein found loosely associated with the inner membrane of the mitochondrion. It belongs to the cytochrome c family of proteins. Cytochrome c is a highly soluble protein, unlike other cytochromes, with a solubility of about 100g/L and is an essential component of the electron transport chain, where it carries one electron. Cytochrome_c | |
| Cytochrome c oxidase enzyme cytochrome c oxidase or Complex IV (, ) is a large transmembrane protein complex found in bacteria and the mitochondrion. It is the last enzyme in the respiratory electron transport chain of mitochondria (or bacteria) located in the mitochondrial (or bacterial) membrane. Cytochrome_c_oxidase | |
| NADH dehydrogenase NADH dehydrogenase () is an enzyme located in the inner mitochondrial membrane that catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NADH_dehydrogenase | |
| Coenzyme Q - cytochrome c reductase The coenzyme Q c — oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (), playing a critical role in biochemical generation of ATP (oxidative phosphorylation). Complex III is a multisubunit transmembrane lipoprotein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits). Coenzyme_Q_-_cytochrome_c_reductase | |
| Xanthine oxidase Xanthine oxidase (XO, a form of xanthine oxidoreductase that generates reactive oxygen species) is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. This enzyme plays an important role in the catabolism of purines in some species, including humans.Xanthine oxidase can be converted to xanthine dehydrogenase by reversible sulfhydryl oxidation. Xanthine_oxidase | |
| Iodothyronine deiodinase Iodothyronine deiodinase () is an enzyme important in the action of thyroid hormones. Deiodinases are unusual in that the enzyme contains selenium, in the form of an otherwise rare amino acid selenocysteine. Iodothyronine_deiodinase |
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