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Viomycin C
Viomycin is a member of the tuberactinomycin family, a group of nonribosomal peptide antibiotics exhibiting anti-tuberculosis activity. The tuberactinomycin family is an essential component in the drug cocktail currently used to fight infections of ''Mycobacterium tuberculosis''. Viomycin was the first member of the tuberactinomycins to be isolated and identified, and was used to treat TB until it was replaced by the less toxic, but structurally related compound, capreomycin. The tuberactinomycins target bacterial ribosomes, binding RNA and disrupting bacterial protein synthesis and certain forms of RNA splicing. Viomycin is produced by the actinomycete '' Streptomyces puniceus''. Biosynthesis The gene cluster for viomycin has been sequenced from ''Streptomyces sp.'' strain ATCC 11861, '' Streptomyces vinaceus'' and from ''Streptomyces lividans'' 1326. It consists of a central cyclic pentapeptide code assembled from nonribosomal peptide synthetase (NRPS). The NRPS contains 4 pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Intramuscular
Intramuscular injection, often abbreviated IM, is the injection of a substance into a muscle. In medicine, it is one of several methods for parenteral administration of medications. Intramuscular injection may be preferred because muscles have larger and more numerous blood vessels than subcutaneous tissue, leading to faster absorption than subcutaneous or intradermal injections. Medication administered via intramuscular injection is not subject to the first-pass metabolism effect which affects oral medications. Common sites for intramuscular injections include the deltoid muscle of the upper arm and the gluteal muscle of the buttock. In infants, the vastus lateralis muscle of the thigh is commonly used. The injection site must be cleaned before administering the injection, and the injection is then administered in a fast, darting motion to decrease the discomfort to the individual. The volume to be injected in the muscle is usually limited to 2–5 milliliters, depending ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ornithine Cyclodeaminase
The enzyme ornithine cyclodeaminase (EC 4.3.1.12) catalyzes the chemical reaction L-ornithine \rightleftharpoons L-proline + NH4+ This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is Lornithine ammonia-lyase (cyclizing; L-proline-forming). Other names in common use include ornithine cyclase, ornithine cyclase (deaminating), and L-ornithine ammonia-lyase (cyclizing). This enzyme participates in arginine and proline biosynthesis. It employs one cofactor, NAD+. Structural studies As of late 2007, two structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made objects such as buildings and machines and natural objects such as ... have been solved for this class of enzymes, with PDB accession codes and . References * * * * * EC 4.3. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polypeptide Antibiotics
Polypeptide antibiotics are a chemically diverse antibiotic classes, class of antibiotics, anti-infective and Chemotherapy#Cytotoxic antibiotics, antitumor antibiotics containing non-protein polypeptide chains. Examples of this class include actinomycin, bacitracin, colistin, and polymyxin B. Actinomycin-D has found use in cancer chemotherapy. Most other polypeptide antibiotics are too toxic for systemic administration, but can safely be administered topically to the skin as an antiseptic for shallow cuts and abrasions. Actinomycin-D is believed to produce its cytotoxic effects by binding DNA and inhibiting RNA synthesis.Cosmegen (dactinomycin for injection) Prescribing Information.Revised: 05/2010, Lundbeck Inc. Other polypeptide antibiotics are thought to mechanism of action, act by permeabilizing the bacterial cell membrane, but the details are largely unknown. Animal studies have shown that actinomycin-D is corrosive to skin, irritating to the eyes and mucous membranes of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Post ModificationsII
Post, POST, or posting may refer to: Postal services * Mail, the postal system, especially in Commonwealth of Nations countries **An Post, the Irish national postal service **Canada Post, Canadian postal service **Deutsche Post, German postal service **Iraqi Post, Iraqi postal service **Russian Post, Russian postal service **Hotel post, a service formerly offered by remote Swiss hotels for the carriage of mail to the nearest official post office **United States Postal Service or USPS **Parcel post, a postal service for mail that is heavier than ordinary letters Work * Post, a job or occupation Newspaper * '' The Manica Post'' Regional newspaper in Manicaland province, Zimbabwe * ''The Rakyat Post'' Malaysian online daily newspaper * ''Bangkok Post'' English language newspaper in Thailand Architecture and structures *Lamppost, a raised source of light on the edge of a road *Post (structural), timber framing *Post and lintel, a building system * Scratch post * Steel fence po ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viomycin BiosynthesisIII
Viomycin is a member of the tuberactinomycin family, a group of nonribosomal peptide antibiotics exhibiting anti-tuberculosis activity. The tuberactinomycin family is an essential component in the drug cocktail currently used to fight infections of ''Mycobacterium tuberculosis''. Viomycin was the first member of the tuberactinomycins to be isolated and identified, and was used to treat TB until it was replaced by the less toxic, but structurally related compound, capreomycin. The tuberactinomycins target bacterial ribosomes, binding RNA and disrupting bacterial protein synthesis and certain forms of RNA splicing. Viomycin is produced by the actinomycete '' Streptomyces puniceus''. Biosynthesis The gene cluster for viomycin has been sequenced from ''Streptomyces sp.'' strain ATCC 11861, '' Streptomyces vinaceus'' and from ''Streptomyces lividans'' 1326. It consists of a central cyclic pentapeptide code assembled from nonribosomal peptide synthetase (NRPS). The NRPS contains 4 pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Genes
In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and non-coding genes. During gene expression (the synthesis of Gene product, RNA or protein from a gene), DNA is first transcription (biology), copied into RNA. RNA can be non-coding RNA, directly functional or be the intermediate protein biosynthesis, template for the synthesis of a protein. The transmission of genes to an organism's offspring, is the basis of the inheritance of phenotypic traits from one generation to the next. These genes make up different DNA sequences, together called a genotype, that is specific to every given individual, within the gene pool of the population (biology), population of a given species. The genotype, along with environmental and developmental factors, ultimately determines the phenotype ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenylation
Adenylylation, more commonly known as AMPylation, is a process in which an adenosine monophosphate (AMP) molecule is covalently attached to the amino acid side chain of a protein. This covalent addition of AMP to a hydroxyl side chain of the protein is a post-translational modification. Adenylylation involves a phosphodiester bond between a hydroxyl group of the molecule undergoing adenylylation, and the phosphate group of the adenosine monophosphate nucleotide (i.e. adenylic acid). Enzymes that are capable of catalyzing this process are called AMPylators. The known amino acids to be targeted in the protein are tyrosine and threonine, and sometimes serine. When charges on a protein undergo a change, it affects the characteristics of the protein, normally by altering its shape via interactions of the amino acids which make up the protein. AMPylation can have various effects on the protein. These are properties of the protein like, stability, enzymatic activity, co-factor binding, and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or Disulfide bond, disulfide bridges. Domains often form functional units, such as the calcium-binding EF-hand, EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimera (protein), chimeric ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biosynthesis
Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-Catalysis, catalyzed processes where chemical substances absorbed as nutrients (or previously converted through biosynthesis) serve as enzyme substrate (chemistry), substrates, with conversion by the living organism either into simpler or more complex Product (chemistry), products. Examples of biosynthetic pathways include those for the production of amino acids, lipid membrane components, and nucleotides, but also for the production of all classes of biological macromolecules, and of acetyl-coenzyme A, adenosine triphosphate, nicotinamide adenine dinucleotide and other key intermediate and transactional molecules needed for metabolism. Thus, in biosynthesis, any of an array of Chemical compound, compounds, from simple to complex, are converted into other compounds, and so it includes both the catabolism and anabolism (building up and breaking down) of comple ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Open Reading Frame
In molecular biology, reading frames are defined as spans of DNA sequence between the start and stop codons. Usually, this is considered within a studied region of a prokaryotic DNA sequence, where only one of the six possible reading frames will be "open" (the "reading", however, refers to the RNA produced by transcription of the DNA and its subsequent interaction with the ribosome in translation). Such an open reading frame (ORF) may contain a start codon (usually AUG in terms of RNA) and by definition cannot extend beyond a stop codon (usually UAA, UAG or UGA in RNA). That start codon (not necessarily the first) indicates where translation may start. The transcription termination site is located after the ORF, beyond the translation stop codon. If transcription were to cease before the stop codon, an incomplete protein would be made during translation. In eukaryotic genes with multiple exons, introns are removed and exons are then joined together after transcription to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aminoglycoside
Aminoglycoside is a medicinal and bacteriologic category of traditional Gram-negative antibacterial medications that inhibit protein synthesis and contain as a portion of the molecule an amino-modified glycoside (sugar). The term can also refer more generally to any organic molecule that contains amino sugar substructures. Aminoglycoside antibiotics display bactericidal activity against Gram-negative aerobes and some anaerobic bacilli where resistance has not yet arisen but generally not against Gram-positive and anaerobic Gram-negative bacteria.ME Levison, MD, 2012, Aminoglycosides, The Merck Manua accessed 22 February 2014. Streptomycin is the first-in-class aminoglycoside antibiotic. It is derived from ''Streptomyces griseus'' and is the earliest modern agent used against tuberculosis. Streptomycin lacks the common 2-deoxystreptamine moiety (image right, below) present in most other members of this class. Other examples of aminoglycosides include the deoxystreptamine-containin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nonribosomal Peptide Synthetase
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] |
