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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 underg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphothreonine
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] |
Proteinogenic
Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 ( selenocysteine and pyrrolysine) that can be incorporated by special translation mechanisms. In contrast, non-proteinogenic amino acids are amino acids that are either not incorporated into proteins (like GABA, L-DOPA, or triiodothyronine), misincorporated in place of a genetically encoded amino acid, or not produced directly and in isolation by standard cellular machinery (like hydroxyproline). The latter often results from post-translational modification of proteins. Some non-proteinogenic amino acids are incorporated into nonribosomal peptides which are synthesized by non-ribosomal peptide synthetases. Both eukaryotes and prokaryotes can incorporate selenocysteine into their ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Essential Amino Acid
An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine. Six other amino acids are considered conditionally essential in the human diet, meaning their synthesis can be limited under special pathophysiological conditions, such as prematurity in the infant or individuals in severe Catabolism, catabolic distress. These six are arginine, cysteine, glycine, glutamine, proline, and tyrosine. Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine, aspartic acid, asparagine, glutamic acid, serine, and selenocysteine (considered the 21st amino acid). Pyrroly ... [...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 l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
William Cumming Rose
William Cumming Rose (April 4, 1887 – September 25, 1985) was an American biochemist and nutritionist. He discovered the amino acid threonine, and his research determined the necessity for essential amino acids in diet and the minimum daily requirements of all amino acids for optimal growth. Early life William Cumming Rose was born in Greenville, South Carolina. He attended various local schools, but his father John M. Rose, who was a Presbyterian minister, began to homeschool William in Latin, Greek, and Hebrew when he was 14 years old. He also studied an introductory chemistry textbook by Ira Remsen. When he was 16, he studied at Davidson College in North Carolina for his bachelor's degree. He took up graduate education at Yale University studying food chemistry with Russell Chittenden and Lafayette Mendel. He was granted a PhD in 1911. Career Rose taught for a time at University of Pennsylvania with Alonzo Taylor. Taylor recommended him to University of Texas Galveston M ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Escherichia Coli
''Escherichia coli'' (),Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. also known as ''E. coli'' (), is a Gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus '' Escherichia'' that is commonly found in the lower intestine of warm-blooded organisms. Most ''E. coli'' strains are harmless, but some serotypes ( EPEC, ETEC etc.) can cause serious food poisoning in their hosts, and are occasionally responsible for food contamination incidents that prompt product recalls. Most strains do not cause disease in humans and are part of the normal microbiota of the gut; such strains are harmless or even beneficial to humans (although these strains tend to be less studied than the pathogenic ones). For example, some strains of ''E. coli'' benefit their hosts by producing vitamin K2 or by preventing the colonization of the intestine by pathogenic bacteria. These mutually beneficial relationships between ''E ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Posttranslational Modification
Post-translational modification (PTM) is the covalent and generally enzymatic modification of proteins following protein biosynthesis. This process occurs in the endoplasmic reticulum and the golgi apparatus. Proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo PTM to form the mature protein product. PTMs are important components in cell signaling, as for example when prohormones are converted to hormones. Post-translational modifications can occur on the amino acid side chains or at the protein's C- or N- termini. They can extend the chemical repertoire of the 20 standard amino acids by modifying an existing functional group or introducing a new one such as phosphate. Phosphorylation is a highly effective mechanism for regulating the activity of enzymes and is the most common post-translational modification. Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called gl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Threonic Acid
Threonic acid is a sugar acid derived from threose. The -isomer is a metabolite of ascorbic acid (vitamin C). One study suggested that because -threonate inhibits DKK1 expression ''in vitro'', it may have potential in treatment of androgenic alopecia. References Sugar acids Alpha hydroxy acids Triols {{organic-compound-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ST Staple
The ST staple is a common four- or five-amino acid residue motif in proteins and polypeptides with serine or threonine as the C-terminal residue. It is characterized by a single hydrogen bond between the hydroxyl group of the serine or threonine (at residue ''i'' + 3 or ''i'' + 4) and the main chain carbonyl In organic chemistry, a carbonyl group is a functional group composed of a carbon atom double-bonded to an oxygen atom: C=O. It is common to several classes of organic compounds, as part of many larger functional groups. A compound containi ... group of residue ''i''. Motifs are of two types, depending whether the motif has 4 or 5 residues. Most ST staples occur in conjunction with an alpha helix, and are usually associated with a slight bend in the helix. Two websites are available for finding and examining ST staples in proteins:Motivated ProteinsanPDBeMotif{{cite journal, last=Golovin, first=A, author2=Henrick K, title=MSDmotif: exploring pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Kinase
In biochemistry, a kinase () is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule. This transesterification produces a phosphorylated substrate and ADP. Conversely, it is referred to as dephosphorylation when the phosphorylated substrate donates a phosphate group and ADP gains a phosphate group (producing a dephosphorylated substrate and the high energy molecule of ATP). These two processes, phosphorylation and dephosphorylation, occur four times during glycolysis. Kinases are part of the larger family of phosphotransferases. Kinases should not be confused with phosphorylases, which catalyze the addition of inorganic phosphate groups to an acceptor, nor with phosphatases, which remove phosphate groups (dephosphorylation). The phosphorylation state of a molecule, whe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monosaccharide
Monosaccharides (from Greek '' monos'': single, '' sacchar'': sugar), also called simple sugars, are the simplest forms of sugar and the most basic units (monomers) from which all carbohydrates are built. They are usually colorless, water- soluble, and crystalline solids. Contrary to their name (sugars), only some monosaccharides have a sweet taste. Most monosaccharides have the formula (though not all molecules with this formula are monosaccharides). Examples of monosaccharides include glucose (dextrose), fructose (levulose), and galactose. Monosaccharides are the building blocks of disaccharides (such as sucrose and lactose) and polysaccharides (such as cellulose and starch). The table sugar used in everyday vernacular is itself a disaccharide sucrose comprising one molecule of each of the two monosaccharides D-glucose and D-fructose. Each carbon atom that supports a hydroxyl group is chiral, except those at the end of the chain. This gives rise to a number of isome ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphorylation
In chemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. This process and its inverse, dephosphorylation, are common in biology and could be driven by natural selection. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License. Protein phosphorylation often activates (or deactivates) many enzymes. Glucose Phosphorylation of sugars is often the first stage in their catabolism. Phosphorylation allows cells to accumulate sugars because the phosphate group prevents the molecules from diffusing back across their transporter. Phosphorylation of glucose is a key reaction in sugar metabolism. The chemical equation for the conversion of D-glucose to D-glucose-6-phosphate in the first step of glycolysis is given by :D-glucose + ATP → D-glucose-6-phosphate + ADP : ΔG° = −16.7 kJ/mol (° indicates measurement at standard condition) Hepatic cells are freely permeable to glucose, and t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
