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Efrapeptin
Efrapeptins are peptides produced by fungi in the genus ''Tolypocladium'' that have antifungal, insecticidal, and mitochondrial ATPase inhibitory activities. They are produced via a biosynthetic pathway similar to but simpler than the Ciclosporin pathway, with nonribosomal peptide synthase (NRPS) and/or polyketide synthase (PKS) being the key elements. The amino acid sequences of efrapeptins are: :Efrapeptin F: Ac-Pip-Aib-Pip-Aib-Aib-Leu-bAla-Gly-Aib-Aib-Pip-Aib-Ala-Leu-Iva-Unk :Efrapeptin G: Ac-Pip-Aib-Pip-Iva-Aib-Leu-bAla-Gly-Aib-Aib-Pip-Aib-Ala-Leu-Iva-Unk ::Aib: 2-methylalanine; Iva: 2-ethylalanine; Unk: does not match to a known amino acid References External links * - Efrapeptin F Efrapeptin Fat ChemSpider ChemSpider is a database of chemicals. ChemSpider is owned by the Royal Society of Chemistry. Database The database contains information on more than 100 million molecules from over 270 data sources including: * EPA DSSTox * U.S. Food and D ... * - Efr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Efrapeptin F
Efrapeptins are peptides produced by fungi in the genus ''Tolypocladium'' that have antifungal, insecticidal, and mitochondrial ATPase inhibitory activities. They are produced via a biosynthetic pathway similar to but simpler than the Ciclosporin pathway, with nonribosomal peptide synthase (NRPS) and/or polyketide synthase (PKS) being the key elements. The amino acid sequences of efrapeptins are: :Efrapeptin F: Ac-Pip-Aib-Pip-Aib-Aib-Leu-bAla-Gly-Aib-Aib-Pip-Aib-Ala-Leu-Iva-Unk :Efrapeptin G: Ac-Pip-Aib-Pip-Iva-Aib-Leu-bAla-Gly-Aib-Aib-Pip-Aib-Ala-Leu-Iva-Unk ::Aib: 2-methylalanine; Iva: 2-ethylalanine; Unk: does not match to a known amino acid References External links * - Efrapeptin F Efrapeptin Fat ChemSpider * - Efrapeptin G Efrapeptin G at ChemSpider Antimicrobial peptides {{organic-chem-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tolypocladium
''Tolypocladium'' is a genus of fungi within the family Ophiocordycipitaceae. It includes species that are parasites of other fungi, insect pathogens, rotifer pathogens and soil inhabiting species with uncertain ecological roles. ''Tolypocladium'' was originally circumscribed as a genus containing anamorphic fungi. It was later determined that some ''Cordyceps''-like teleomorphic fungi were the teleomorphs of ''Tolypocladium'' species. These species were considered to belong in the genus ''Cordyceps'' until molecular phylogenetics studies found these species to be more closely related to ''Ophiocordyceps'' and were considered to belong in that genus before they were transferred to the new genus ''Elaphocordyceps'' by Sung and colleagues in 2007. However, under the ICN's 2011 " one fungus, one name" principle, fungi can not have different names for their anamorphic and teleomorphic stages if they are found to be the same taxon. Quandt and colleagues formally synonymized ''Tolypocl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ATPase
ATPases (, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3−-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life. Some such enzymes are integral membrane proteins (anchored within biological membranes), and move solutes across the membrane, typically against their concentration gradient. These are called transmembrane ATPases. Functions Transmembrane ATPases import metabolites necessary for cell metabolism and export toxins, wastes, and solutes that can hinder cellular processes. An important example is the sodium-potass ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ciclosporin
Ciclosporin, also spelled cyclosporine and cyclosporin, is a calcineurin inhibitor, used as an immunosuppressant medication. It is a natural product. It is taken orally or intravenously for rheumatoid arthritis, psoriasis, Crohn's disease, nephrotic syndrome, and in organ transplants to prevent rejection. It is also used as eye drops for keratoconjunctivitis sicca (dry eyes). Common side effects include high blood pressure, headache, kidney problems, increased hair growth, and vomiting. Other severe side effects include an increased risk of infection, liver problems, and an increased risk of lymphoma. Blood levels of the medication should be checked to decrease the risk of side effects. Use during pregnancy may result in preterm birth; however, ciclosporin does not appear to cause birth defects. Ciclosporin is believed to work by decreasing the function of lymphocytes. It does this by forming a complex with cyclophilin to block the phosphatase activity of calcineurin, w ... [...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] |
Polyketide Synthase
Polyketides are a class of natural products derived from a precursor molecule consisting of a chain of alternating ketone (or reduced forms of a ketone) and methylene groups: (-CO-CH2-). First studied in the early 20th century, discovery, biosynthesis, and application of polyketides has evolved. It is a large and diverse group of secondary metabolites caused by its complex biosynthesis which resembles that of fatty acid synthesis. Because of this diversity, polyketides can have various medicinal, agricultural, and industrial applications. Many polyketides are medicinal or exhibit acute toxicity. Biotechnology has enabled discovery of more naturally-occurring polyketides and evolution of new polyketides with novel or improved bioactivity. History Naturally produced polyketides by various plants and organisms have been used by humans since before studies on them began in the 19th and 20th century. In 1893, J. Norman Collie synthesized detectable amounts of orcinol by heating dehy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ChemSpider
ChemSpider is a database of chemicals. ChemSpider is owned by the Royal Society of Chemistry. Database The database contains information on more than 100 million molecules from over 270 data sources including: * EPA DSSTox * U.S. Food and Drug Administration (FDA) * Human Metabolome Database * Journal of Heterocyclic Chemistry * KEGG * KUMGM * LeadScope * LipidMAPS * Marinlit * MDPI * MICAD * MLSMR * MMDB * MOLI * MTDP * Nanogen * Nature Chemical Biology * NCGC * NIAID * National Institutes of Health (NIH) * NINDS Approved Drug Screening Program * NIST * NIST Chemistry WebBook * NMMLSC * NMRShiftDB * PANACHE * PCMD * PDSP * Peptides * Prous Science Drugs of the Future * QSAR * R&D Chemicals * San Diego Center for Chemical Genomics * SGCOxCompounds, SGCStoCompounds * SMID * Specs * Structural Genomics Consortium * SureChem * Synthon-Lab * Thomson Pharma * Total TOSLab Building-Blocks * UM-BBD * UPCMLD * UsefulChem * Web of Science * xPharm Each chemical is given a unique i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
