Fumitremorgin
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Fumitremorgin
Fumitremorgin A-C Fumitremorgins are tremorogenic metabolites of '' Aspergillus'' and '' Penicillium'', that belong to a class of naturally occurring 2,5-diketopiperazines. Biosynthesis Biosynthesis pathway of fumitremorgin pathway involves several different enzymes. FtmA is a nonribosomal peptide synthase. Both FtmB and FtmH are prenyltransferase. Three different cytochrome P450 monooxygenases involved in the biosynthesis of furmitremorgin C are FtmC, FtmE, and FtmG. Furthermore, FtmD is proposed to function as the methyltransferase. The synthesis starts with the formation of brevianamide F. FtmA catalyzes the nonribosomal peptide synthesis (NRPS) of this diketopiperazine product from two amino acids, L-tryptophan and L-proline Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the prot .. ...
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Fumitremorgin A-C
Fumitremorgin A-C Fumitremorgins are tremorogenic metabolites of '' Aspergillus'' and '' Penicillium'', that belong to a class of naturally occurring 2,5-diketopiperazines. Biosynthesis Biosynthesis pathway of fumitremorgin pathway involves several different enzymes. FtmA is a nonribosomal peptide synthase. Both FtmB and FtmH are prenyltransferase. Three different cytochrome P450 monooxygenases involved in the biosynthesis of furmitremorgin C are FtmC, FtmE, and FtmG. Furthermore, FtmD is proposed to function as the methyltransferase. The synthesis starts with the formation of brevianamide F. FtmA catalyzes the nonribosomal peptide synthesis (NRPS) of this diketopiperazine product from two amino acids, L-tryptophan and L-proline. Then, another enzyme, FtmB, prenylates the product to form tryprostatin B. At this point, there are two separate pathways. FtmE may cyclize tryprostatin B to form demethoxyfumitremorgin C, or FtmC may oxidize tryprostatin B to form desmethyltrprostati ...
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Aspergillus
'''' () is a genus consisting of several hundred mold species found in various climates worldwide. ''Aspergillus'' was first catalogued in 1729 by the Italian priest and biologist Pier Antonio Micheli. Viewing the fungi under a microscope, Micheli was reminded of the shape of an ''aspergillum'' (holy water sprinkler), from Latin ''spargere'' (to sprinkle), and named the genus accordingly. Aspergillum is an asexual spore-forming structure common to all ''Aspergillus'' species; around one-third of species are also known to have a sexual stage. While some species of ''Aspergillus'' are known to cause fungal infections, others are of commercial importance. Taxonomy Species ''Aspergillus'' consists of 837 species of fungi. Growth and distribution ''Aspergillus'' is defined as a group of conidial fungi—that is, fungi in an asexual state. Some of them, however, are known to have a teleomorph (sexual state) in the Ascomycota. With DNA evidence, all members of the genus '' ...
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Penicillium
''Penicillium'' () is a genus of ascomycetous fungi that is part of the mycobiome of many species and is of major importance in the natural environment, in food spoilage, and in food and drug production. Some members of the genus produce penicillin, a molecule that is used as an antibiotic, which kills or stops the growth of certain kinds of bacteria. Other species are used in cheesemaking. According to the ''Dictionary of the Fungi'' (10th edition, 2008), the widespread genus contains over 300 species. Taxonomy The genus was first described in the scientific literature by Johann Heinrich Friedrich Link in his 1809 work ''Observationes in ordines plantarum naturales''; he wrote, "''Penicillium. Thallus e floccis caespitosis septatis simplicibus aut ramosis fertilibus erectis apice penicillatis''", where ''penicillatis'' means "having tufts of fine hair". Link included three species—'' P. candidum'', '' P. expansum'', and '' P. glaucum''—all of which produ ...
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Proposed Biosynthesis Pathway
Proposal(s) or The Proposal may refer to: * Proposal (business) * Research proposal * Proposal (marriage) * Proposition, a proposal in logic and philosophy Arts, entertainment, and media * ''The Proposal'' (album) Films * ''The Proposal'' (1957 film), an Australian television play based on Chekhov's 1890 play * ''The Proposal'' (2001 film), starring Nick Moran, Jennifer Esposito, and Stephen Lang * ''The Proposal'' (2009 film), starring Sandra Bullock and Ryan Reynolds * ''The Proposal'' (2022 film), starring Joe Joseph and Amara Raja * " La propuesta" ("The Proposal"), a short story in the 2014 Argentina anthology film ''Wild Tales'' Literature * '' Proposals (play)'', a 1997 play by Neil Simon * ''The Proposal'' (novel), 1999 and 35th book in the ''Animorphs'' series by K.A. Applegate * ''The Proposal'', alternative title of Chekhov's 1890 play ''A Marriage Proposal'' Television * ''The Proposal'' (American TV series), a 2018 reality dating series * The Proposal ( ...
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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 " ...
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Prenyltransferase
Prenyltransferases (PTs) are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to isoprenyl diphosphate syntheses (IPPSs). Prenyltransferases are a functional category and include several enzyme groups that are evolutionarily independent. Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereochemistry of the resulting products. Examples of trans-prenyltranferases include dimethylallyltranstransferase, and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to dolichol). Trans- and cis-prenyltransferases are evolutionarily unrelated to each other and there is no sequential and structural similarity. The beta subunit of the farnesyltransferases is responsible for peptide binding. Squalene-hopene cyclase is a bacterial enzyme that catalyzes the cyclization of squalene ...
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Cytochrome P450
Cytochromes P450 (CYPs) are a Protein superfamily, superfamily of enzymes containing heme as a cofactor (biochemistry), cofactor that functions as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance (pharmacology), clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Ronald W. Estabrook, Estabrook, David Y. Cooper, Cooper, and Otto Rosenthal, Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of secondary metabolite, defensive compounds, fatty acids, and hormones. CYP enzymes have been identified in all kingdom (biology), kingdoms of life: animals, plants, fungus, fungi, protists, bacteria, and archaea, as well as in viruses. However, they are not omnipresent; for example, they have not been found in ''Escherichia coli''. , more than 300,000 distinct CYP proteins ...
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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 ...
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L-tryptophan
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an Alpha_and_beta_carbon , α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar Aromatic hydrocarbon, aromatic Alpha and beta carbon, beta carbon substituent. It is Essential amino acid, 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 Genetic code, 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 deprotonation, 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 ...
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L-proline
Proline (symbol Pro or P) is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group but is rather a secondary amine. The secondary amine nitrogen is in the protonated form (NH2+) under biological conditions, while the carboxyl group is in the deprotonated −COO− form. The "side chain" from the α carbon connects to the nitrogen forming a pyrrolidine loop, classifying it as a aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting with CC (CCU, CCC, CCA, and CCG). Proline is the only proteinogenic secondary amino acid which is a secondary amine, as the nitrogen atom is attached both to the α-carbon and to a chain of three carbons that together form a five-membered ring. History and etymology Proline was first isolated in 1900 by Richard Willstätter who obtained the amino a ...
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Indole
Indole is an aromatic heterocyclic organic compound with the formula C8 H7 N. It has a bicyclic structure, consisting of a six-membered benzene ring fused to a five-membered pyrrole ring. Indole is widely distributed in the natural environment and can be produced by a variety of bacteria. As an intercellular signal molecule, indole regulates various aspects of bacterial physiology, including spore formation, plasmid stability, resistance to drugs, biofilm formation, and virulence. The amino acid tryptophan is an indole derivative and the precursor of the neurotransmitter serotonin. General properties and occurrence Indole is a solid at room temperature. It occurs naturally in human feces and has an intense fecal odor. At very low concentrations, however, it has a flowery smell, and is a constituent of many perfumes. It also occurs in coal tar. The corresponding substituent is called indolyl. Indole undergoes electrophilic substitution, mainly at position 3 (see diagra ...
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