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Ergotamine Tartrate
Ergotamine, sold under the brand names Cafergot (with caffeine) and Ergomar among others, is an ergopeptine and part of the ergot family of alkaloids; it is structurally and biochemically closely related to ergoline. It possesses structural similarity to several neurotransmitters, and has biological activity as a vasoconstrictor. It is used medicinally for treatment of acute migraine attacks (sometimes in combination with caffeine). Medicinal usage of ergot fungus began in the 16th century to induce childbirth, yet dosage uncertainties discouraged the use. It has been used to prevent post-partum hemorrhage (bleeding after childbirth). It was first isolated from the ergot fungus by Arthur Stoll at Sandoz in 1918 and marketed as Gynergen in 1921. Biosynthesis Ergotamine is a secondary metabolite (natural product) and the principal alkaloid produced by the ergot fungus, ''Claviceps purpurea'', and related fungi in the family Clavicipitaceae. Its biosynthesis in these fungi requir ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cafergot
Caffeine/ergotamine (trade name Cafergot) is the proprietary name of a medication consisting of ergotamine tartrate and caffeine. This combination is used for the treatment of headaches, such as migraine headache. Use Correct timing of use is important. Cafergot is an abortive headache treatment, which prevents the development of the headache, rather than a treatment for an established headache. The medication should be administered at the first sign of headache. There exist some limitations as to the maximum number of tablets that can be taken per day per week. Different sources of drug information may carry different information, and patients are encouraged to ask their pharmacist or prescriber about such details. Cafergot is currently available as a generic drug (ergotamine tartrate/caffeine) Mechanism of action According to a topic review on UpToDate, "ergotamine and dihydroergotamine (DHE 45) bind to 5HT 1b/d receptors, just as triptans do." This along with binding to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sandoz
Novartis AG is a Swiss-American multinational pharmaceutical corporation based in Basel, Switzerland and Cambridge, Massachusetts, United States (global research).name="novartis.com">https://www.novartis.com/research-development/research-locations It is one of the largest pharmaceutical companies in the world. Novartis manufactures the drugs clozapine (Clozaril), diclofenac (Voltaren; sold to GlaxoSmithKline in 2015 deal), carbamazepine (Tegretol), valsartan (Diovan), imatinib mesylate (Gleevec/Glivec), cyclosporine (Neoral/Sandimmune), letrozole (Femara), methylphenidate (Ritalin; production ceased 2020), terbinafine (Lamisil), deferasirox (Exjade), and others. In March 1996, the companies Ciba-Geigy and Sandoz merged to form Novartis; the pharmaceutical and agrochemical divisions of both companies formed Novartis as an independent entity. Other Ciba-Geigy and Sandoz businesses were sold, or, like Ciba Specialty Chemicals, spun off as independent companies. The Sandoz brand ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nonribosomal Peptide
Nonribosomal peptides (NRP) are a class of peptide secondary metabolites, usually produced by microorganisms like bacteria and fungi. Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. While there exist a wide range of peptides that are not synthesized by ribosomes, the term ''nonribosomal peptide'' typically refers to a very specific set of these as discussed in this article. Nonribosomal peptides are synthesized by nonribosomal peptide synthetases, which, unlike the ribosomes, are independent of messenger RNA. Each nonribosomal peptide synthetase can synthesize only one type of peptide. Nonribosomal peptides often have cyclic and/or branched structures, can contain non-proteinogenic amino acids including D-amino acids, carry modifications like '' N''-methyl and ''N''-formyl groups, or are glycosylated, acylated, halogenated, or hydroxylated. Cyclization of amino acids against the peptide " ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lysergic Acid
Lysergic acid, also known as -lysergic acid and (+)-lysergic acid, is a precursor for a wide range of ergoline alkaloids that are produced by the ergot fungus and found in the seeds of '' Turbina corymbosa'' (ololiuhqui), '' Argyreia nervosa'' (Hawaiian baby woodrose), and ''Ipomoea tricolor'' (morning glories, tlitliltzin). Amides of lysergic acid, lysergamides, are widely used as pharmaceuticals and as psychedelic drugs (LSD). Lysergic acid is listed as a Table I precursor under the United Nations Convention Against Illicit Traffic in Narcotic Drugs and Psychotropic Substances. Lysergic acid received its name as it was a product of the lysis of various ergot alkaloids. Total synthesis Lysergic acid is generally produced by hydrolysis of natural lysergamides, but can also be synthesized in the laboratory by a complex total synthesis, for example by Robert Burns Woodward's team in 1956. An enantioselective total synthesis based on a palladium-catalyzed domino cyclization r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxygenase
An oxygenase is any enzyme that oxidizes a substrate by transferring the oxygen from molecular oxygen O2 (as in air) to it. The oxygenases form a class of oxidoreductases; their EC number is EC 1.13 or EC 1.14. Discoverers Oxygenases were discovered in 1955 simultaneously by two groups, Osamu Hayaishi from Japan and Howard S. Mason from the US. Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance." Chemical Makeup Oxygenases consist of both constitutive and inducible isozymes (HO-1, HO-2). These constitute a major intracellular source of iron and carbon monoxide Types There are two types of oxygenases: *Monooxygenases, or mixed function oxidase, transfer one oxygen atom to the substrate, and reduce the other oxygen atom to water. *Dioxygenases, or oxygen transferases, incorporate both atoms of molecular oxygen (O2) into the product(s) of the reaction. Among the most impor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methyltransferase
Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding ''S''-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leavi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prenylation
Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or a biomolecule. It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed. Prenyl groups (also called isoprenyl groups, having one hydrogen atom more than isoprene) have been shown to be important for protein–protein binding through specialized prenyl-binding domains. Protein prenylation Protein prenylation involves the transfer of either a farnesyl or a geranylgeranyl moiety to C-terminal cysteine(s) of the target protein. There are three enzymes that carry out prenylation in the cell, farnesyl transferase, Caax protease and geranylgeranyl transferase I. Farnesylation is a type of prenylation, a post-translational modification of proteins by which an isoprenyl group is added to a cysteine residue. It is an important pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tryptophan Dimethylallyltransferase
In enzymology, a tryptophan dimethylallyltransferase () is an enzyme that catalysis, catalyzes the chemical reaction :dimethylallyl diphosphate + L-tryptophan \rightleftharpoons diphosphate + 4-(3-methylbut-2-enyl)-L-tryptophan Thus, the two substrate (biochemistry), substrates of this enzyme are dimethylallyl diphosphate and L-tryptophan, whereas its two product (chemistry), products are diphosphate and 4-(3-methylbut-2-enyl)-L-tryptophan. This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The List of enzymes, systematic name of this enzyme class is . Other names in common use include , , , DMAT synthetase, and . References * EC 2.5.1 Enzymes of unknown structure {{2.5-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dimethylallyl Pyrophosphate
Dimethylallyl pyrophosphate (DMAPP; or alternatively, dimethylallyl diphosphate (DMADP); also isoprenyl pyrophosphate) is an isoprenoid precursor. It is a product of both the mevalonate pathway and the MEP pathway of isoprenoid precursor biosynthesis. It is an isomer of isopentenyl pyrophosphate (IPP) and exists in virtually all life forms. The enzyme isopentenyl pyrophosphate isomerase catalyzes isomerization between DMAPP and IPP. In the mevalonate pathway DMAPP is synthesised from mevalonic acid. In contrast, DMAPP is synthesised from HMBPP in the MEP pathway. At present, it is believed that there is crossover between the two pathways in organisms that use both pathways to create terpenes and terpenoid The terpenoids, also known as isoprenoids, are a class of naturally occurring organic chemicals derived from the 5-carbon compound isoprene and its derivatives called terpenes, diterpenes, etc. While sometimes used interchangeably with "terpenes" ...s, such as in plants, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tryptophan
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α- carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. It is essential in humans, meaning that the body cannot synthesize it and it must be obtained from the diet. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3. It is encoded by the codon UGG. Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–; pKa = 9.39) and the carboxylic acid is deprotonated ( –COO−; pKa = 2.38). Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. Function Amino acids, including tryptophan, are used as building blocks in protein biosynthesis, and proteins are required to sustain life. Man ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha amino acids appear in the genetic code. Amino acids can be classified according to the locations of the core structural functional groups, as Alpha and beta carbon, alpha- , beta- , gamma- or delta- amino acids; other categories relate to Chemical polarity, polarity, ionization, and side chain group type (aliphatic, Open-chain compound, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Clavicipitaceae
The Clavicipitaceae are a family of fungi within the order Hypocreales. A 2008 estimate placed 43 genera in the family, but recent work has increased this number to 97. Phylogeny Molecular phylogenetic analysis of multigene DNA sequence data indicates the taxon Clavicipitaceae is paraphyletic, and consists of three well-defined clades, at least one of which is shared with members of another fungal family (Hypocreaceae). The evolution within the Clavicipitaceae is marked by interkingdom host jumping, and the range of this large and heterogeneous fungal group spans mutualistic plant symbionts, as well as parasites of plants, insects, and other fungi. Significance Many of its members produce alkaloids toxic to animals and humans. One of its most infamous species is ''Claviceps purpurea'', which has historical significance as the cause of St. Anthony's fire, also known as ergotism. Ergotism is caused by ergot alkaloids, such as ergotamine and ergocristine, which are chemical d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
