Fluorothreonine
4-Fluoro--threonine is an antibacterial produced by '' Streptomyces cattleya''. It is formed by the fluorothreonine transaldolase catalysed transfer of fluoroacetaldehyde Fluoroacetaldehyde is a metabolic precursor of both fluoroacetate and 4-fluorothreonine in ''Streptomyces cattleya''. References {{reflist Organofluorides Aldehydes Fluorine-containing natural products ... onto threonine. References Fluorinated amino acids Fluorohydrins Fluorine-containing natural products {{organic-compound-stub ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Fluorothreonine Transaldolase
In enzymology, a fluorothreonine transaldolase () is an enzyme that catalyzes the chemical reaction :L-threonine + fluoroacetaldehyde \rightleftharpoons acetaldehyde + 4-fluoro-L-threonine Thus, the two substrates of this enzyme are L-threonine and fluoroacetaldehyde, whereas its two products are acetaldehyde and 4-fluoro-L-threonine. This enzyme belongs to the family of transferases, specifically those transferring aldehyde or ketonic groups (transaldolases and transketolases, respectively). The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivial ... of this enzyme class is fluoroacetaldehyde:L-threonine aldehydetransferase. References * * EC 2.2.1 Enzymes of unknown structure {{transferase-stub ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Fluoroacetaldehyde
Fluoroacetaldehyde is a metabolic precursor of both fluoroacetate and 4-fluorothreonine in ''Streptomyces cattleya ''Streptomyces cattleya'' is a Gram-positive bacterium which makes cephamycin, penicillin and thienamycin. The bacterium expresses a fluorinase enzyme, and the organism has been used to understand the biosynthesis of fluoroacetate and the antibac ...''. References {{reflist Organofluorides Aldehydes Fluorine-containing natural products ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Streptomyces Cattleya
{{Streptomyces-stub ...
''Streptomyces cattleya'' is a Gram-positive bacterium which makes cephamycin, penicillin and thienamycin. The bacterium expresses a fluorinase enzyme, and the organism has been used to understand the biosynthesis of fluoroacetate and the antibacterial 4-fluoro-L-threonine. The γ-Glu-βes pathway to biosynthesis of non-traditional amino acids β-ethynylserine (βes) and L-propargylglycine (Pra) was first characterized in this species. The genome, which was sequenced in 2011, contains one chromosome with 6,283,062 base pairs and one megaplasmid with 1,809,491 bp, with an overall guanine-cytosine content of 73%. References cattleya ''Cattleya'' () is a genus of orchids from Costa Rica south to Argentina. The genus is abbreviated C in trade journals. Description Epiphytic or terrestrial orchids with cylindrical rhizome from which the fleshy noodle-like roots grow. Pseu ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Threonine
Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), a carboxyl group (which is in the deprotonated −COO− form under biological conditions), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as ''E. coli''. It is encoded by all the codons starting AC (ACU, ACC, ACA, and ACG). Threonine sidechains are often hydrogen bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples (usually at the middle of alpha helices). Modifications The threonine residue is susceptible to numerous posttranslational modifications. The hydroxyl side-chain can unde ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
|
Fluorinated Amino Acids
In chemistry, halogenation is a chemical reaction that entails the introduction of one or more halogens into a compound. Halide-containing compounds are pervasive, making this type of transformation important, e.g. in the production of polymers, drugs. This kind of conversion is in fact so common that a comprehensive overview is challenging. This article mainly deals with halogenation using elemental halogens (F2, Cl2, Br2, I2). Halides are also commonly introduced using salts of the halides and halogen acids. Many specialized reagents exist for and introducing halogens into diverse substrates, e.g. thionyl chloride. Organic chemistry Several pathways exist for the halogenation of organic compounds, including free radical halogenation, ketone halogenation, electrophilic halogenation, and halogen addition reaction. The nature of the substrate determines the pathway. The facility of halogenation is influenced by the halogen. Fluorine and chlorine are more electrophilic and are m ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |