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Glycocyamine
Glycocyamine (or guanidinoacetate) is a metabolite of glycine in which the amino group has been converted into a guanidine by guanylation (transfer of a guanidine group from arginine). In vertebrate organism it is then transformed into creatine by methylation. Glycocyamine is used as a supplement and as a feed additive in poultry farming. However, the metabolism of creatine from glycocyamine in the liver causes a depletion of methyl groups. This causes homocysteine levels to rise, which has been shown to produce cardiovascular and skeletal problems. Glycocyamine plays a role in the metabolism of the amino acids serine, threonine and proline. Production Biochemical synthesis Glycocyamine is formed in the mammalian organism primarily in the kidneys by transferring the guanidine group of L-arginine by the enzyme L-Arg:Gly-amidinotransferase (AGAT) to the amino acid glycine. From L-arginine, ornithine is thus produced, which is metabolized in the urea cycle by carbamoylation to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sarcosine
Sarcosine, also known as ''N''-methylglycine, or monomethylglycine, is a monopeptide with the formula CH3N(H)CH2CO2H. It exists at neutral pH as the zwitterion CH3N+(H)2CH2CO2−, which can be obtained as a white, water-soluble powder. Like some amino acids, sarcosine converts to a cation at low pH and an anion at high pH, with the respective formulas CH3N+(H)2CH2CO2H and CH3N(H)CH2CO2−. Sarcosine is a close relative of glycine, with a secondary amine in place of the primary amine. Sarcosine is ubiquitous in biological materials. It is used in manufacturing biodegradable surfactants and toothpastes as well as in other applications. Sarcosine is sweet to the taste. Biochemistry Sarcosine is an intermediate and byproduct in glycine synthesis and degradation. Sarcosine is metabolized to glycine by the enzyme sarcosine dehydrogenase, while glycine-''N''-methyl transferase generates sarcosine from glycine. Sarcosine is an amino acid derivative that is naturally found in muscles ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Creatine
Creatine ( or ) is an organic compound with the nominal formula (H2N)(HN)CN(CH3)CH2CO2H. It exists in various modifications (tautomers) in solution. Creatine is found in vertebrates where it facilitates recycling of adenosine triphosphate (ATP), primarily in muscle and brain tissue. Recycling is achieved by converting adenosine diphosphate (ADP) back to ATP via donation of phosphate groups. Creatine also acts as a buffer. History Creatine was first identified in 1832 when Michel Eugène Chevreul isolated it from the basified water-extract of skeletal muscle. He later named the crystallized precipitate after the Greek word for meat, κρέας (''kreas''). In 1928, creatine was shown to exist in equilibrium with creatinine. Studies in the 1920s showed that consumption of large amounts of creatine did not result in its excretion. This result pointed to the ability of the body to store creatine, which in turn suggested its use as a dietary supplement. In 1912, Harvard Univer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Creatine
Creatine ( or ) is an organic compound with the nominal formula (H2N)(HN)CN(CH3)CH2CO2H. It exists in various modifications (tautomers) in solution. Creatine is found in vertebrates where it facilitates recycling of adenosine triphosphate (ATP), primarily in muscle and brain tissue. Recycling is achieved by converting adenosine diphosphate (ADP) back to ATP via donation of phosphate groups. Creatine also acts as a buffer. History Creatine was first identified in 1832 when Michel Eugène Chevreul isolated it from the basified water-extract of skeletal muscle. He later named the crystallized precipitate after the Greek word for meat, κρέας (''kreas''). In 1928, creatine was shown to exist in equilibrium with creatinine. Studies in the 1920s showed that consumption of large amounts of creatine did not result in its excretion. This result pointed to the ability of the body to store creatine, which in turn suggested its use as a dietary supplement. In 1912, Harvard Univer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Dimethylglycine
Dimethylglycine (DMG) is a derivative of the amino acid glycine with the structural formula (CH3)2NCH2COOH. It can be found in beans and liver, and has a sweet taste. It can be formed from trimethylglycine upon the loss of one of its methyl groups. It is also a byproduct of the metabolism of choline. When DMG was first discovered, it was referred to as Vitamin B16, but, unlike true B vitamins, deficiency of DMG in the diet does not lead to any ill-effects and it is synthesized by the human body in the citric acid cycle meaning it does not meet the definition of a vitamin. Uses Dimethylglycine has been suggested for use as an athletic performance enhancer, immunostimulant, and a treatment for autism, epilepsy, or mitochondrial disease. There is no evidence that dimethylglycine is effective for treating mitochondrial disease. Published studies on the subject have shown little to no difference between DMG treatment and placebo in autism spectrum disorders. Biological activity Dime ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta-Methylamino-L-alanine
β-Methylamino--alanine, or BMAA, is a non-proteinogenic amino acid produced by cyanobacteria. BMAA is a neurotoxin and its potential role in various neurodegenerative disorders is the subject of scientific research. Structure and properties BMAA is a derivative of the amino acid alanine with a methylamino group on the side chain. This non-proteinogenic amino acid is classified as a polar base. Sources and detection BMAA is produced by cyanobacteria in marine, freshwater, and terrestrial environments. In cultured non-nitrogen-fixing cyanobacteria, BMAA production increases in a nitrogen-depleted medium. The biosynthetic pathway in cyanobacteria is unknown, but involvement of BMAA and its structural analog 2,4-diaminobutanoic acid (2,4-DAB) in envioronmental iron scavenging has been hypothesized. BMAA has been found in aquatic organisms and in plants with cyanobacterial symbionts such as certain lichens, the floating fern ''Azolla'', the leaf petioles of the tropical fl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Guanidinopropionic Acid
β-Guanidinopropionic acid, also referred to as guanidinopropionic acid, beta-guanidinopropionic acid or β-GPA, is a dietary supplement. β-Guanidinopropionic acid is a white crystalline powder soluble in water (50 mg/ml-clear, colorless solution). Studies on animals (rats, monkeys, hamsters) show that acidic guanidine derivatives such as β-GPA can ameliorate hyperglycemia Hyperglycemia is a condition in which an excessive amount of glucose circulates in the blood plasma. This is generally a blood sugar level higher than 11.1 mmol/L (200 mg/dL), but symptoms may not start to become noticeable until even ... in animal models of noninsulin-dependent diabetes. Though the oral availability of β-GPA is well established, the basic uptake mechanism has not been studied yet. References {{reflist Guanidines Carboxylic acids ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine Amidinotransferase
L-Arginine:glycine amidinotransferase (AGAT; ) is the enzyme that catalyses the transfer of an amidino group from L-arginine to glycine. The products are L-ornithine and glycocyamine, also known as guanidinoacetate, the immediate precursor of creatine. Creatine and its phosphorylated form play a central role in the energy metabolism of muscle and nerve tissues. Creatine is in highest concentrations in the skeletal muscle, heart, spermatozoa and photoreceptor cells. Creatine helps buffer the rapid changes in ADP/ ATP ratio in muscle and nerve cells during active periods. Creatine is also synthesized in other tissues, such as pancreas, kidneys, and liver, where amidinotransferase is located in the cytoplasm, including the intermembrane space of the mitochondria, of the cells that make up those tissues. Function L-Arginine:glycine amidinotransferase catalyses the first, which is also the committed step in the formation of creatine. The second step of the process, producing the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ornithine
Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl. Role in urea cycle L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a central part of the urea cycle, which allows for the disposal of excess nitrogen. Ornithine is recycled and, in a manner, is a catalyst. First, ammonia is converted into carbamoyl phosphate (). Ornithine is converted into a urea derivative at the δ (terminal) nitrogen by carbamoyl phosphate synthetase. Another nitrogen is added from aspartate, producing the denitrogenated fumarate, and the resulting arginine (a guanidinium compound) is hydrolysed back to ornithine, producing urea. The nitrogens of urea come from the ammonia and aspartate, and the nitrogen in ornithine remains intact. Ornithine is not an amino acid coded for by DNA, that is, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Urea Cycle
The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH2)2CO from ammonia (NH3). Animals that use this cycle, mainly amphibians and mammals, are called ureotelic. The urea cycle converts highly toxic ammonia to urea for excretion. This cycle was the first metabolic cycle to be discovered ( Hans Krebs and Kurt Henseleit, 1932), five years before the discovery of the TCA cycle. This cycle was described in more detail later on by Ratner and Cohen. The urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. Function Amino acid catabolism results in waste ammonia. All animals need a way to excrete this product. Most aquatic organisms, or ammonotelic organisms, excrete ammonia without converting it. Organisms that cannot easily and safely remove nitrogen as ammonia convert it to a less toxic substance, such as urea, via the urea cycle, which occurs mainly in the liver. Urea produced by the liver is th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Citrulline
The organic compound citrulline is an α-amino acid. Its name is derived from ''citrullus'', the Latin word for watermelon. Although named and described by gastroenterologists since the late 19th century, it was first isolated from watermelon in 1914 by Japanese researchers Yotaro Koga and Ryo OdakeEarly references spell Ryo Odake's name as ''Ryo Othake''. and further codified by Mitsunori Wada of Tokyo Imperial University in 1930. It has the formula H2NC(O)NH(CH2)3CH(NH2)CO2H. It is a key intermediate in the urea cycle, the pathway by which mammals excrete ammonia by converting it into urea. Citrulline is also produced as a byproduct of the enzymatic production of nitric oxide from the amino acid arginine, catalyzed by nitric oxide synthase. Biosynthesis Citrulline can be derived from: * from arginine via nitric oxide synthase, as a byproduct of the production of nitric oxide for signaling purposes * from ornithine through the breakdown of proline or glutamine/glutamate * from ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
S-Adenosyl Methionine
''S''-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. More than 40 methyl transfers from SAM are known, to various substrates such as nucleic acids, proteins, lipids and secondary metabolites. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by Giulio Cantoni in 1952. In bacteria, SAM is bound by the SAM riboswitch, which regulates genes involved in methionine or cysteine biosynthesis. In eukaryotic cells, SAM serves as a regulator of a variety of processes including DNA, tRNA, and rRNA methylation; immune response; amino acid metabolism; transsulfuration; and more. In plants, SAM is crucial to the biosynthesis of ethylene, an important plant hormone and sig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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