GLYCINE

GLYCINE ( GLİSİN )

Glycine (short for Gly or G) is an apolar amino acid with the formula NH2CH2COOH. Glycine codons GGU, GGC, GGA, GGG cf. It is the genetic code. Structurally, it is the simplest of the 20 amino acids found in proteins. Its side chain consists of only one hydrogen atom. Since the α-carbon atom in glycine is also bound to a hydrogen, glycine is not optically active, ie it has no optical isomers.

CAS NO : 56-40-6

SYNONYMS:

Glycine ; 2-Aminoacetic acid ; 56-40-6 ; aminoacetic acid ; Glycocoll ; Aminoethanoic acid ; Glycolixir ; Padil ; Glycosthene ; Aciport ; Glicoamin ; L-Glycine ; H-Gly-OH ; Hampshire glycine ; Amitone ; Leimzucker ; Acetic acid, amino- ;Aminoazijnzuur ; Glycine, non-medical , Sucre de gelatine ;Gyn-hydralin ; GLY (IUPAC abbrev) ; Glycinum ; Corilin ; Glycinum [INN-Latin] ;Glicina [INN-Spanish] Glycine [INN] ; glycyl radical ; Glyzin ; FEMA No. 3287 ; gly ; Acide aminoacetique [INN-French] ;Acido aminoacetico [INN-Spanish] ; Acidum aminoaceticum [INN-Latin] ; CCRIS 5915 ; HSDB 495 ; AI3-04085 ; amino-Acetic acid ; UNII-TE7660XO1C ; MFCD00008131 ; NSC 25936 ; [14C]glycine ; GLYCINE 1.5% IN PLASTIC CONTAINER ; EINECS 200-272-2 ; CHEMBL773 ; AMINOACETIC ACID 1.5% IN PLASTIC CONTAINER ; Glycine iron sulphate (1:1) ; TE7660XO1C ; CHEBI:15428 ; 2-aminoaceticacid ; AZD-4282 ; NSC25936 ; Athenon ; NSC-25936 ; 25718-94-9 ; polyglycine ; NCGC00024503-01 ; Glicina ; DSSTox_CID_667 ; Glycine, free base ; Polyglycine II ; Acido aminoacetico ; Acide aminoacetique ; DSSTox_RID_75720 ; DSSTox_GSID_20667 ; Acidum aminoaceticum ; Glycine, 99%, ACS reagent ; Glycine, 99+%, for analysis ; Glykokoll ; Aminoessigsaeure ; Hgly ; CAS-56-40-6 ; Glycine, labeled with carbon-14 ; Glycine [USP:INN] ; H2N-CH2-COOH ; Glycine, homopolymer (VAN) ; Aminoethanoate ; amino-Acetate ; 2-aminoacetate ; Glycine; ; glycine USP ; Glycine Technical ; glycine-13c ; [3H]glycine Glycine, EP/USP ; H-Gly ; L-Gly ; Gly-CO ; Gly-OH ; L-Glycine,(S) ; [14C]-glycine ; Corilin (Salt/Mix) ; Glycine 1 M solution ; PubChem18924 ; Tocris-0219 ; Glycine (H-Gly-OH) ; NH2CH2COOH ; Glycine, >=99% ; Aminoacetic acid,medicinal ; Glycine (JP17/USP) ; Glycine, 99%, FCC ; Biomol-NT_000195 bmse000089 ; bmse000977 ; WLN: Z1VQ ; EC 200-272-2 ; H-[15N]Gly-OH ; Gly-253 ; GTPL727; AB-131/40217813 ; KSC205S9D ; Glycine, Electrophoresis Grade ; BPBio1_001222 ; GTPL4084 ; GTPL4635 N[C]C(O)=O ; DTXSID9020667 ; BDBM18133 ; Buffer Concentrate, pH 11.01 ; CTK1A5991 ; H-Gly-OH 56-40-6 ; Glycine, >=99.0% (NT) ; Glycine, 98.5-101.5% ; Pharmakon1600-01300021 ; 2-Aminoacetic acid;Aminoacetic acid ; BCP25965 ; CS-B1641 ; HY-Y0966 ; KS-000002MW ; ZINC4658552 ; Glycine, ACS reagent, >=98.5% ; Tox21_113575 ; 2-amino-1-$l^{1}-oxidanylethanone ; ANW-32505 ; Glycine, 99%, natural, FCC, FG ; LS-218 ; NSC760120 ; s4821 ; STL194276 ; Glycine, purum, >=98.5% (NT) Glycine, tested according to Ph.Eur. ; AKOS000119626 ; Glycine, for electrophoresis, >=99% ; Tox21_113575_1 ; AM81781 ; CCG-266010 ; DB00145 ; MCULE-2415764032 ; NSC-76012 ; Glycine, BioUltra, >=99.0% (NT) ; Glycine, BioXtra, >=99% (titration) ; Glycine, SAJ special grade, >=99.0% NCGC00024503-02 ; NCGC0002; SC-26884 ; Glycine, 0.2M buffer solution, pH 2.5 ; Glycine, 0.2M buffer solution, pH 3.0 ; Glycine, 0.2M buffer solution, pH 3.5 ; DB-029870 ; FT-0600491 ; FT-0669038 G0099 ; G0317 ; Glycine, ReagentPlus(R), >=99% (HPLC) ; A20662 ; C00037 ; D00011 ; M-6155 ; M03001 ; L001246 ; Q620730 ; SR-01000597729 ; Glycine, certified reference material, TraceCERT(R) Q-201300 ; SR-01000597729-1 ; Q27115084 ; B72BA06C-60E9-4A83-A24A-A2D7F465BB65 ; F2191-0197 ; Glycine, European Pharmacopoeia (EP) Reference Standard ; Z955123660 ; Glycine, BioUltra, for molecular biology, >=99.0% (NT) ; UNII-0O72R8RF8A component DHMQDGOQFOQNFH-UHFFFAOYSA-N ; Glycine, United States Pharmacopeia (USP) Reference Standard ; Glycine, Pharmaceutical Secondary Standard; Certified Reference Material ; Tris-tricine buffer; Tris-glycine buffer;Tris glycine buffer concentrate ; Glycine, analytical standard, for nitrogen determination according to Kjeldahl method ; Glycine, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, >=98.5% ; Glycine, meets analytical specification of Ph. Eur., BP, USP, 99-101% (based on anhydrous substance) ; Glycine, PharmaGrade, Ajinomoto, EP, JP, USP, manufactured under appropriate GMP controls for Pharma or Biopharmaceutical production, suitable for cell culture ; Glycine, puriss. p.a., Reag. Ph. Eur., buffer substance, 99.7-101% (calc. to the dried substance)

Glycine is a non-essential, non-polar, non-optical, glucogenic amino acid. Glycine, an inhibitory neurotransmitter in the CNS, triggers chloride ion influx via ionotropic receptors, thereby creating an inhibitory post-synaptic potential. In contrast, this agent also acts as a co-agonist, along with glutamate, facilitating an excitatory potential at the glutaminergic N-methyl-D-aspartic acid (NMDA) receptors. Glycine is an important component and precursor for many macromolecules in the cells.

Glycine is the simplest (and the only achiral) proteinogenic amino acid, with a hydrogen atom as its side chain. It has a role as a nutraceutical, a hepatoprotective agent, an EC 2.1.2.1 (glycine hydroxymethyltransferase) inhibitor, a NMDA receptor agonist, a micronutrient, a fundamental metabolite and a neurotransmitter. It is an alpha-amino acid, a serine family amino acid and a proteinogenic amino acid. It is a conjugate base of a glycinium. It is a conjugate acid of a glycinate. It is a tautomer of a glycine zwitterion. Betaine is a modified amino acid consisting of glycine with three methyl groups that serves as a methyl donor in several metabolic pathways and is used to treat the rare genetic causes of homocystinuria. Betaine has had only limited clinical use, but has not been linked to instances of serum enzyme elevations during therapy or to clinically apparent liver injury.

 This substance is registered under the REACH Regulation and is manufactured in and / or imported to the European Economic Area, at ≥ 1 000 to < 10 000 tonnes per annum.

This substance is used by consumers, in articles, by professional workers (widespread uses), in formulation or re-packing, at industrial sites and in manufacturing. This substance is used in the following products: washing & cleaning products, cosmetics and personal care products, perfumes and fragrances, adhesives and sealants, coating products, anti-freeze products, fillers, putties, plasters, modelling clay, polishes and waxes, biocides (e.g. disinfectants, pest control products), lubricants and greases, air care products and leather treatment products.

Other release to the environment of this substance is likely to occur from: indoor use (e.g. machine wash liquids/detergents, automotive care products, paints and coating or adhesives, fragrances and air fresheners) and outdoor use.  Release to the environment of this substance can occur from industrial use: industrial abrasion processing with low release rate (e.g. cutting of textile, cutting, machining or grinding of metal) and of articles where the substances are not intended to be released and where the conditions of use do not promote release. Other release to the environment of this substance is likely to occur from: outdoor use in long-life materials with low release rate (e.g. metal, wooden and plastic construction and building materials), indoor use in long-life materials with low release rate (e.g. flooring, furniture, toys, construction materials, curtains, foot-wear, leather products, paper and cardboard products, electronic equipment), indoor use in long-life materials with high release rate (e.g. release from fabrics, textiles during washing, removal of indoor paints) and outdoor use in long-life materials with high release rate (e.g. tyres, treated wooden products, treated textile and fabric, brake pads in trucks or cars, sanding of buildings (bridges, facades) or vehicles (ships)). This substance can be found in complex articles, with no release intended: vehicles and machinery, mechanical appliances and electrical/electronic products (e.g. computers, cameras, lamps, refrigerators, washing machines). This substance can be found in products with material based on: metal (e.g. cutlery, pots, toys, jewellery) and plastic (e.g. food packaging and storage, toys, mobile phones). This substance is intended to be released from scented: clothes, paper products and CDs. This substance is used in the following products: washing & cleaning products, lubricants and greases, laboratory chemicals, adhesives and sealants, coating products, biocides (e.g. disinfectants, pest control products), polishes and waxes, air care products and cosmetics and personal care products. Glycine is used in the following areas: health services, agriculture, forestry and fishing, municipal supply (e.g. electricity, steam, gas, water) and sewage treatment and scientific research and development. This substance is used for the manufacture of: food products, chemicals, metals and fabricated metal products. Other release to the environment of this substance is likely to occur from: indoor use (e.g. machine wash liquids/detergents, automotive care products, paints and coating or adhesives, fragrances and air fresheners) and outdoor use. Glycine  is used in the following products: cosmetics and personal care products, laboratory chemicals, pharmaceuticals and coating products. Release to the environment of this substance can occur from industrial use: formulation of mixtures. Glycine  is used in the following products: pharmaceuticals, washing & cleaning products, laboratory chemicals, pH regulators and water treatment products, perfumes and fragrances and cosmetics and personal care products. Glycine  is used in the following areas: health services, formulation of mixtures and/or re-packaging, scientific research and development, agriculture, forestry and fishing and mining. Glycine  is used for the manufacture of: chemicals, electrical, electronic and optical equipment and food products. Release to the environment of this substance can occur from industrial use: as an intermediate step in further manufacturing of another substance (use of intermediates), in the production of articles, in processing aids at industrial sites and as processing aid. Glycine is of the simplest structure in the 20 members of amino acid series, also known as amino acetate. It is a non-essential amino acid for the human body and contains both acidic and basic functional group inside its molecule. It exhibits as a strong electrolyte an aqueous solution, and has a large solubility in strong polar solvents but almost insoluble in non-polar solvents. Moreover, it also has a relative high melting point and boiling point. The adjustment of the pH of the aqueous solution can make glycine exhibit different molecular forms. The side chain of glycine contains only a hydrogen atom. Owing to another hydrogen atom connecting to the α-carbon atom, the glycine is not optical isomer. Since the side bond of glycine is very small, it can occupy space which can’t be occupied by other amino acids, such as those amino acids located within the collagen helix. At room temperature, it exhibits as white crystal or light yellow crystalline powder and has a unique sweet taste which can ease the taste of acid and alkaline taste, masking the bitter taste of saccharin in food and enhance the sweetness. However, if an excessive amount of glycine is absorbed by body, they not only can’t be totally absorbed by the body, but will also break the balance of the body's absorption of amino acids as well as affect the absorption of other kinds of amino acids, leading to nutrient imbalances and negatively affected health. The milk drink with glycine being the major raw material can easily does harm to the normal growth and development of young people and children. It has a density of 1.1607, melting point of 232~236 °C (decomposition). It is soluble in water but insoluble in alcohol and ether. It is capable of acting together with hydrochloric acid to form hydrochloride salt. It is presented in the muscles of animals. IT can be produced from the reaction between monochloro acetate and ammonium hydroxide as well as from the hydrolysis of gelation with further refining. Amino acids are organic acids containing an amino group and are the basic units of protein. They are generally colorless crystals with a relative high melting point (over 200 °C). It is soluble in water with amphiprotic ionization characteristics and can have sensitive colorimetric reaction with ninhydrin reagent. In 1820, glycine with the simplest structure was first discovered in a protein hydrolysis product. Until 1940, it has been found that there were about 20 kinds of amino acids in nature. They are necessary for the protein synthesis of both human and animal. They are mostly α-L-type amino acids. According to the different number of amino groups and carboxyl groups contained in amino acids, we classify amino acids into neutral amino acids (glycine, alanine, leucine, isoleucine, valine, cystine, cysteine, A methionine, threonine, serine, phenylalanine, tyrosine, tryptophan, proline and hydroxyproline, etc.) with the amino acid molecules containing only one amino group and a carboxyl group; acidic amino acid (glutamate, aspartate) which contains two carboxyl and one amino group; alkaline amino acids (lysine, arginine) which molecularly contains one carboxyl group and two amino groups; Histidine contains a nitrogen ring which exhibits weakly alkaline and thus also belonging to alkaline amino acids. Amino acids can be obtained both from protein hydrolysis and from chemical synthesis. Since the 1960s, industrial production mainly applied microbial fermentation, such as monosodium glutamate factory has been widely applied fermentation method for production of glutamate. In recent years, people has also applied petroleum hydrocarbons and other chemical products as raw materials of fermentation for production of amino acids. The above information is edited by the Chemicalbook of Dai Xiongfeng. Accurately weigh 175 mg of sample which has undergone drying for 2 h at 105 °C and place it in a 250m1 flask, add 50 mL of glacial acetic acid for dissolving; add 2 drops of crystal violet test solution (TS-74); titrate with 0.1ml/L perchloric acid to blue-green endpoint. At the same time carry out a blank test, and make the necessary corrections. Each mL of 0.1mol/L perchloric acid is equivalent to glycine (C2H5NO2) 7.507mg. In the late 1980s, Japan's Mitsubishi Corporation added the screened aerobic Agrobacterium, Brevibacterium, Corynebacterium genus to the medium containing carbon, nitrogen and inorganic nutrient solution for cultivation, and then applied this class of bacteria for converting ethanolamine to glycine in 25~45 °C and pH value from 4 to 9 and further applied concentration, neutralization ion exchange treatment to get the glycine product. After entering the 1990s, there had been new progress on the production technology of glycine in foreign countries. The Nitto Chemical Industry Co (Japan) add cultured pseudomonas genus, casein bacteria genus, and alcaligenes genus and other species in 0.5% (mass fraction, dry weight) to the glycine amine-containing matrix for reaction of 45 h under 30 °C and pH value of 7.9 to 8.1 with almost all glycine amine being hydrolyzed into glycine with the conversion rate of 99%. Although biological methods are still in the research stage, however, owing to its high selectivity, non-pollution property, it will be a synthetic route with highly development potential. Used for the pharmaceutical industry, organic synthesis and biochemical analysis. Used as a buffer for the preparation of tissue culture media and the testing of copper, gold and silver. In medicine, it is used for the treatment of myasthenia gravis and progressive muscular atrophy, hyperacidity, chronic enteritis, and children hyperprolinemia diseases. Used for the treatment of myasthenia gravis and progressive muscular atrophy; treatment of excess stomach acid ester disease, chronic enteritis (often in combination antacid); using in combination with aspirin can reduce the irritation of the stomach; treatment of children hyperprolinemia; as the nitrogen source for generating non-essential amino acid and can be added to a mixed amino acid injection. Glycine is primarily used as a nutritional additive in chicken feed. Used as a kind of nutritional supplement which is mainly used for flavoring. Flavoring agent: Used for alcoholic beverage in combination with alanine; the addition amount: grape wine: 0.4%, whiskey: 0.2%, champagne: 1.0%. Others such as powder soup: 2%; lees marinated foods: 1%. Because it is tasted like shrimp and cuttlefish, and thus can be used in sauces. It has some certain inhibitory effects on the Bacillus subtilis and E. coli and thus can be used as the preservatives of surimi products and peanut butter with the added amount being 1% to 2%.

Buffering effect: Because glycine is amphiprotic ions containing both amino and carboxyl groups, it has a strong buffering property on the taste feeling of salt and vinegar. The added amount is: salted products: 0.3% to 0.7%, acid stain product: 0.05% to 0.5%. Antioxidant effect (with its metal chelation): being added to butter, cheese, and margarine extend the storage duration by 3 to 4 times. To make the lard oil in baked food be stable, we can add 2.5% glucose and 0.5% glycine. Adding 0.1% to 0.5% glycine to the wheat flour for making convenient noodles can play a role of flavoring. In pharmacy, it is used as antacids (hyperacidity), therapeutic agent for muscle nutritional disorder as well as antidotes. Moreover, glycine can also be used as the raw material for synthesizing amino acids like threonine. It can be used as a spice according to the provisions of GB 2760-96. Glycine is also known as aminoacetic acid. In the field of pesticide production, it is used for synthesizing the glycine ethyl ester hydrochloride which is the intermediate for the synthesis of pyrethroid insecticides. Moreover, it can also be used for synthesizing fungicides iprodione and solid glyphosate herbicide; in addition it is also used in various kinds of other industries such as fertilizer, medicine, food additives, and spices. Used as a solvent to remove carbon dioxide in the fertilizer industry. In the pharmaceutical industry, it can be used as amino acid preparations, the buffer of chlortetracycline buffer and as the raw material for synthesizing the anti-Parkinson's disease drugs L-dopa. Moreover, it is also the intermediate for producing ethyl imidazole. It is also an adjunct therapy medicine for treating neural hyperacidity and effectively suppressing excess amount of gastric ulcer acid. In the food industry, it is used for the synthesis of alcohol, brewing products, meat processing and cold drinks formula. As a food additive, glycine can be used alone as a condiment and also used in combination with sodium glutamate, DL-alanine acid, and citric acid. In other industries, it can be used as a pH adjusting agent, being added to the plating solution, or used as the raw material for making other amino acids. It can further be used as biochemical reagents and solvent in organic synthesis and biochemistry. Used as the intermediates of pharmaceutical and pesticide, decarbonation solvents of fertilizers, plating fluid, etc. Used as a solvent for removing carbon dioxide in the fertilizer industry. In pharmaceutical industry, it is used as the buffer of chlortetracycline, amino antacids, and used for the preparation of L-dopa. In food industry, it can be used as flavoring agents, agent for removing saccharine bitter taste, for brewing, meat processing, and preparation of soft drinks. In addition, it can also be used as a pH adjusting agent and used in the preparation of the plating solution. Used as biochemical reagents for the pharmaceutical, food and feed additives; it can also be used as a non-toxic decarbonization agent in the field of fertilizer industry.            Glycine (abbreviated as Gly or G) is an organic compound with the formula NH2CH2COOH. Having a hydrogen substituent as its side-chain, glycine is the smallest of the 20 amino acids commonly found in proteins. Its codons are GGU, GGC, GGA, GGG of the genetic code. Glycine is a colourless, sweet-tasting crystalline solid. It is unique among the proteinogenic amino acids in that it is not chiral. It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. Glycine is also the genus name of the Soybean plant (species name = Glycine max). A white, odorless, crystalline powder having a sweetish taste. Its solution is acid to litmus. One g dissolves in about 4 mL of water. It is very slightly soluble in alcohol and in ether. Glycine may be prepared from chloroacetic acid and ammonia; from protein sources, such as gelatin and silk fibroin; from ammonium bicarbonate and sodium cyanide; by catalytic cleavage of serine; from hydrobromic acid and methyleneaminoacetonitrile. Glycine is odorless and has a slightly sweet taste. Glycine occurs as a white, odorless, crystalline powder, and has a sweet taste. Gelatin and silk fbroin are reportedly the best natural sources of this amino acid. glycine is an amino acid used as a texturizer in cosmetic formulations. It makes up approximately 30 percent of the collagen molecule. Glycine is a nonessential amino acid that functions as a nutrient and dietary supplement. it has a solubility of 1 g in 4 ml of water and is abundant in collagen. it is used to mask the bitter aftertaste of sac- charin, for example, in artificially sweetened soft drinks. it retards rancidity in fat.  Non-essential amino acid for human development. An inhibitory neurotransmitter in spinal cord, allosteric regulator of NMDA receptors. Glycine is a non-essential amino acid for human development. Glycine is an inhibitory neurotransmitter in spinal cord, allosteric regulator of NMDA receptors. In the US, glycine is typically sold in two grades: United States Pharmacopeia (“USP”), and technical grade. Most glycine is manufactured as USP grade material for diverse uses. USP grade sales account for approximately 80 to 85 percent of the U.S. market for glycine. Pharmaceutical grade glycine is produced for some pharmaceutical applications, such as intravenous injections, where the customer’s purity requirements often exceed the minimum required under the USP grade designation. Pharmaceutical grade glycine is often produced to proprietary specifications and is typically sold at a premium over USP grade glycine. Technical grade glycine, which may or may not meet USP grade standards, is sold for use in industrial applications; e.g., as an agent in metal complexing and finishing. Technical grade glycine is typically sold at a discount to USP grade glycine. Animal and human foods Other markets for USP grade glycine include its use an additive in pet food and animal feed. For humans, glycine is sold as a sweetener/taste enhancer. Certain food supplements and protein drinks contain glycine. Certain drug formulations include glycine to improve gastric absorption of the drug. Cosmetics and miscellaneous applications. Glycine serves as a buffering agent in antacids, analgesics, antiperspirants, cosmetics, and toiletries. Many miscellaneous products use glycine or its derivatives, such as the production of rubber sponge products, fertilizers, metal complexants. Chemical feed stock Glycine is an intermediate in the synthesis of a variety of chemical products. It is used in the manufacture of the herbicide glyphosate. Glyphosate is a non-selective systemic herbicide used to kill weeds, especially perennials and broadcast or used in the cutstump treatment as a forestry herbicide. Glycine was discovered in 1820, by Henri Braconnot who boiled gelatin with sulfuric acid. Glycine is manufactured industrially by treating chloroacetic acid with ammonia : ClCH2COOH + 2 NH3→H2NCH2COOH + NH4Cl About 15 million kg are produced annually in this way. In the USA (by GEO Specialty Chemicals, Inc.) and in Japan (by Shoadenko), glycine is produced via the Strecker amino acid synthesis. Chemical synthesis is the most suitable method of preparation of glycine. Amination of chloroacetic acid and the hydrolysis of aminoacetonitrile are the favored methods of production. From chloroacetic acid and ammonia; from protein sources, such as gelatin and silk fbroin; from ammonium bicarbonate and sodium cyanide; by catalytic cleavage of serine; from hydrobromic acid and methyleneaminoacetonitrile.  ChEBI: The simplest (and the only achiral) proteinogenic amino acid, with a hydrogen atom as its side chain. Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine, which is in turn derived from 3-phospho glycerate. In most organisms, the enzyme Serine hydroxy methyl transferase catalyses this transformation via the cofactor pyridoxal phosphate : serine + tetra hydro folate → glycine +N5,N10-Methylene tetrahydrofolate + H2O In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme). This conversion is readily reversible : CO2 + NH4+ + N5,N10-Methylene tetra hydro folate + NADH + H+→ Glycine + tetrahydrofolate +NAD+ Glycine is coded by codons GGU, GGC, GGA and GGG. Most proteins incorporate only small quantities of glycine. A notable exception is collagen, which contains about 35 % glycine. Glycine is manufactured exclusively by chemical synthesis, and two main processes are practiced today. The direct amination of chloroacetic acid with a large excess of ammonia gives good yields of glycine without producing large amounts of di- and trialkylated products. This process is widely used in China, where the main application of the glycine is as a raw material for the herbicide glyphosate. The other main process is the Strecker synthesis. The direct Strecker reaction of formaldehyde and ammonium cyanide produces methylene amino acetonitrile, which must be hydrolyzed in two stages to produce glycine . A more efficient approach is to aminate the intermediate glycolonitrile, followed by hydrolysis]. An alternative method, which is more often applied for the homologous amino acids, is the Bucherer–Bergs reaction. Reaction of formaldehyde and ammonium carbonate or bicarbonate gives the intermediate hydantoin, which can be hydrolyzed to glycine in a separate step. Glycine is manufactured exclusively by chemical synthesis, and two main processes are practiced today. The direct amination of chloroacetic acid with a large excess of ammonia gives good yields of glycine without producing large amounts of di- and trialkylated products. This process is widely used in China, where the main application of the glycine is as a raw material for the herbicide glyphosate. The other main process is the Strecker synthesis. The direct Strecker reaction of formaldehyde and ammonium cyanide produces methylene amino acetonitrile, which must be hydrolyzed in two stages to produce glycine . A more efficient approach is to aminate the intermediate glycolonitrile, followed by hydrolysis]. An alternative method, which is more often applied for the homologous amino acids, is the Bucherer–Bergs reaction. Reaction of formaldehyde and ammonium carbonate or bicarbonate gives the intermediate hydantoin, which can be hydrolyzed to glycine in a separate step. Glycine is another inhibitory CNS neurotransmitter. Whereas GABA is located primarily in the brain, glycine is found predominantly in the ventral horn of the spinal cord. Relatively few drugs are known to interact with glycine; the best-known example is the convulsant agent strychnine, which appears to be a relatively specific antagonist of glycine. Glycine is routinely used as a cofreeze-dried excipient in protein formulations owing to its ability to form a strong, porous, and elegant cake structure in the final lyophilized product. It is one of the most frequently utilized excipients in freeze-dried injectable formulations owing to its advantageous freeze-drying properties. Glycine has been investigated as a disintegration accelerant in fast-disintegrating formulations owing to its excellent wetting nature.It is also used as a buffering agent and conditioner in cosmetics. Glycine may be used along with antacids in the treatment of gastric hyperacidity, and it may also be included in aspirin preparations to aid the reduction of gastric irritation. Glycine is the simplest naturally occurring amino acid and is a constituent of most proteins. Its formula is H2N·CH2·COOH. One of the major inhibitory neurotransmitters in the mammalian CNS, predominantly active in the spinal cord and brain stem. Also acts as a modulator of excitatory amino acid transmission mediated by NMDA receptors. Also available as part of the NMDA Receptor - Glycine Site Tocriset™ . Moderately toxic by intravenous route. Mildly toxic by ingestion. Mutation data reported. When heated to decomposition it emits toxic fumes of NOx.  Glycine is used as a sweetener, buffering agent, and dietary supplement. The pure form of glycine is moderately toxic by the IV route and mildly toxic by ingestion. Systemic absorption of glycine irrigation solutions can lead to disturbances of fluid and electrolyte balance and cardiovascular and pulmonary disorders. Glycine starts to decompose at 233°C. Store in well-closed containers. Glycine irrigation solutions (95–105% glycine) should be stored in single dose containers, preferably type I or type II glass.  o, and draining the crystals centrifugally. Alternatively, crystallise it from distilled water by addition of MeOH or EtOH (e.g. 50g dissolved in 100mL of warm water, and 400mL of MeOH is added). The crystals are washed with MeOH or EtOH, then with diethyl ether. Likely impurities are ammonium glycinate, iminodiacetic acid, nitrilotriacetic acid or/and ammonium chloride. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 p 1955 1961, Beilstein 4 IV 2349.] Glycine is degraded via three pathways. The predominant pathway in animals and plants involves the glycine cleavage enzyme Glycine + tetra hydro folate + NAD+ → CO2 + NH4+ + N5,N10-Methylene tetra hydrofolate + NADH + H+ In the second pathway, glycine is degraded in two steps. The first step is the reverse of glycine biosynthesis from serine with serine hydroxymethyl transferase. Serine is then converted to pyruvate by serine dehydratase. In the third pathway of glycine degradation, glycine is converted to glyoxylate by D-amino acid oxidase. Glyoxylate is then oxidized by hepatic lactate dehydrogenase to oxalate in an NAD+-dependent reaction. The half-life of glycine and its elimination from the body varies significantly based on dose. In one study, the half-life was between 0.5 and 4.0 hou. The detection of glycine in the interstellar medium has been debated . In 2008, the glycine - like molecule amino aceto nitrile was discovered in the Large Molecule Heimat, a giant gas cloud near the galactic center in the constellation Sagittarius by the Max Planck Institute for Radio Astronomy . In 2009, glycine sampled in 2004 from comet Wild 2 by the NASA spacecraft Stardust was confirmed, the first discovery of extraterrestrial glycine. That mission's results bolstered the theory of panspermia, which claims that the "seeds" of life are widespread throughout the universe. Glycine may undergo Maillard reactions with amino acids to produce yellowing or browning. Reducing sugars will also interact with secondary amines to form an imine, but without any accompanying yellow-brown discoloration.    GRAS listed. Accepted for use as a food additive in Europe. Included in the FDA Inactive Ingredients Database (IM, IV, SC injections; oral; rectal) and approved for irrigant solutions. Included in parenteral (powders for injection; solutions for injection; vaccines; kits for implant) and nonparenteral (orodispersible tablets/oral lyophilizate; powders for inhalation; powders for oral solution; tablets) formulations licensed in the UK. They form parts of the two polypeptide main chains (or the same polypeptide segment) where they can get quite close to each other due to the lack of side chains. Also, glycine is much more flexible than other amino acids, so it is the parts where the main chain moves or even breaks. Since glycine is the smallest amino acid, it can fit in many places where other amino acids cannot. For example, only glycine of the amino acids can be found in the collagen helix. Glycine is evolutionarily conserved at certain positions of some proteins (eg cytochrome c, myoglobin and hemoglobin). Because mutations that replace glycine with a larger amino acid completely disrupt the structure of these proteins. Glycine is a colorless, sweetish crystalline solid. Proteins generally contain a small number of glycine building blocks. Collagen, which is one third of glycine, is an exception. Glycine is industrially produced from the reaction of chloroacetic acid with ammonia: [3]ClCH2COOH + 2 NH3 → H2NCH2COOH + NH4Cl Approximately 15 million kg of glycine is produced annually in this way. [4] In America (GEO Specialty Chemicals, Inc.) and Japan (Showa Denko), glycine Strecker is produced by amino acid synthesis. The pKA value of glycine is between 2.35 and 9.78. If the pH is above 9.78, most of the glycine is in the form of anionic amine (H2NCH2CO2-). Below pH 2.35, the glycine solution mostly contains cationic carboxylic acid (H3N + CH2CO2H). The isoelectric point of glycine is 6.06. Glycine exists in solution as a zwitterion. In this case, the partial charges in different atoms determined using the Gasteiger charge method are given as follows: N (+0.2358), H (bound to the N atom) (+0.1964), alpha-C (+0.001853), H (bound to the alpha-C atom) (+0.08799), carbonyl C (+0.085) and carbonyl O (-0.5445). Glycine is an intermediate product used in the synthesis of various chemical products. It is used in the production of herbicides with glyphosate effective substances. Glyphosate is a non-selective systemic herbicide that kills weeds. It is used as a forest herbicide to dry the underground part of especially seedy and perennial or cut trees. Although glyphosate was first sold by Monsanto under the Roundup trademark, it is now marketed by many companies as it is no longer under patent.  Glycine is an inhibitory neurotransmitter in the central nervous system, especially in the spinal cord, brain stem and retina. When glycine receptors on neurons are stimulated by glycine, Cl- flux occurs into the neuron via ionotropic receptors. The accumulation of negatively charged ions in the neuron causes an inhibitory postsynaptic potential. The neuron becomes more difficult to stimulate. Strychnine is an effective antagonist on ionotropic glycine receptors. Since glycine can be synthesized by the cells of the human body in sufficient amounts to meet physiological needs, it is not necessary to take it from the diet. Glycine is an amino acid that your body uses to create proteins, which it needs for the growth and maintenance of tissue and for making important substances, such as hormones and enzymes. Your body naturally produces glycine from other amino acids, but it’s also found in protein-rich foods and available as a dietary supplement. Along with being a component of protein, glycine has several other impressive health benefits. Glycine is an amino acid, or a building block for protein. The body can make glycine on its own, but it is also consumed in the diet. A typical diet contains about 2 grams of glycine daily. The primary sources are protein-rich foods including meat, fish, dairy, and legumes. Glycine can also be taken as a supplement.

Glycine is used for schizophrenia, stroke, and memory and thinking skills (cognitive function), but there is no good scientific evidence to support these uses. The body uses glycine to make proteins. Glycine is also involved in the transmission of chemical signals in the brain, so there is interest in trying it for schizophrenia and improving memory. Some researchers think glycine may have a role in cancer prevention because it seems to interfere with the blood supply needed by certain tumors. Schizophrenia. Taking glycine by mouth along with conventional medicines seems to reduce certain symptoms of schizophrenia, called negative symptoms, in some people who don't respond to treatment with conventional medicines Stroke. Taking glycine under the tongue for 5 days may help to reduce brain damage due to a stroke that was caused by the blockage of a blood vessel (usually by a clot) in the brain. A rare, inherited disorder that prevents the body from making the amino acid serine (3-PGDH deficiency). 3-PGDH deficiency is a rare condition in which serine is not synthesized properly. Taking glycine by mouth might reduce seizures in people with this condition.Memory and thinking skills (cognitive function). Early research shows that taking glycine by mouth might improve memory and mental performance. Cystic fibrosis. Early research shows that t king glycine by mouth might improve lung function and breathing by a small amount in patients with cystic fibrosis. Glycine, the simplest amino acid, obtainable by hydrolysis of proteins. Sweet-tasting, it was among the earliest amino acids to be isolated from gelatin (1820). Especially rich sources include gelatin and silk fibroin. Glycine is one of several so-called nonessential amino acids for mammals; i.e., they can synthesize it from the amino acids serine and threonine and from other sources and do not require dietary sources. The chemical structure of glycine is glycine, chemical compound This article was most recently revised and updated by Erik Gregersen, Senior Editor. protein synthesi protein: Structures of common amino acid The simplest amino acid is glycine, in which R is a hydrogen atom. In a number of amino acids, R represents straight or branched carbon chains. One of these amino acids is alanine, in which R is the methyl group (―CH3). Valine, leucine, neuron; conduction of the action potentia nervous system: Amino acid Unlike GABA, glycine is found mostly at lower levels of the central nervous system, including the spinal cord, medulla oblongata, and pons. It is a major inhibitor released by interneurons to suppress motoneuronal activity. Like GABA, glycine acts by increasing Cl− conductance at the postsynaptic membrane, although photosynthesis photosynthesis: Evolution of the process (condensation) of the amino acid glycine and the fatty acid acetate may have formed complex organic molecules known as porphyrins. These molecules, in turn, may have evolved further into coloured molecules called pigments—e.g., chlorophylls of green plants newsletter icon. Glycine can be metabolized to glyoxylate, a precursor of oxalate. Intravenous infusion of 1 liter of 2.2% glycine, 1.5% glycine + 1% ethanol, or 5% mannitol on 13 occasions in five healthy volunteers and glycine irrigation in nine patients undergoing transurethral prostatic did not increase urinary oxalate concentrations [33]. In 10 male volunteers there was no change in urinary excretion of oxalate, calcium, or citrate after an intravenous infusion of glycine 22 g, although urine volume and amino acid excretion increased [34]. However, of 34 patients who received glycine irrigation during and soon after transurethral prostatectomy three developed hyponatremia accompanied by severe hyperoxaluria, with raised urinary glycolate concentrations. Glycine is an important postsynaptic inhibitory neurotransmitter in the CNS. Glycinergic neurons exist chiefly as small interneurons in the ventral (anterior) horn of the spinal cord (i.e., Renshaw cells) and the brainstem. They are proposed to function as a rheostat to dampen brainstem and spinal reflexes that involve the somatic motor system. The main glycine receptor is a Cl−channel, so its activation will promote membrane hyperpolarization and reduce neuronal responsiveness. Glycine activity in the synapse is quenched by reuptake via specific transporters into presynaptic terminals and perisynaptic glial cells. The glia can release glycine, suggesting that glycine from this source may also serve as a neuromodulator. Some inhibitory synapses can simultaneously release GABA and glycine. During development, glycine may act transiently as an excitatory transmitter to help guide the maturation of CNS neurons. Glycine is an amino acid commonly found in proteins. It is synthesized in the body from serine, another proteinogenic amino acid naturally synthesized within cells. As one of the 20 most common amino acids found in proteins, it serves multiple metabolic functions, but some of it is also released into synapses as a neurotransmitter.

Levels of glycine are primarily regulated by enzymatic degradation. Various enzymes are responsible for the breakdown of glycine. Some of these processes reverse the metabolism of glycine and convert the amino acid back to serine. Other enzymatic processes transform glycine into other molecules, including gloxylic acid. Like glutamate and GABA, glycine is present in the nervous system and is an important building block for many chemical processes. As a neurotransmitter, it binds to several families of ionotropic and metabotropic receptors, but its primary inhibitory action seems to be the result of regulating chloride channels in a manner similar to the action of GABA. These effects are primarily seen in the spinal cord. In the brain, the effects of glycine are less predictable. For example, it seems to be involved in regulating glutamatergic neurotransmission at the NMDA glutamate ionotropic receptors that are involved in opening calcium channels and causing rapid depolarization of the post-synaptic cell. Thus, glycine may be an alosteric modulator for glutamate. Increase in glycine function may result in effects similar to the increase of GABAergic neurotransmission (fatigue, drowsiness, etc.). However, since glycine seems to have varying effects in different parts of the brain, supplementation with glycine may also result in excitatory effects. For example, in overdose, glycine causes death by hyperexcitability of the brain. Supplementation with glycine seems to offer limited benefits, although some preliminary evidence exists that it may be helpful in treating the symptoms of psychosis (as discussed in Chapter 11). Inhibition of glycine action is also associated with serious risks. Strichnine is a potent glycine antagonist, and causes muscular convulsions and death by asphyxia. In smaller doses, it was once used as a stimulant. Interestingly, bicuculine is a weaker antagonist that seems to exert its effect by antagonizing glycine and GABA. Thus, the effects of the inhibition of glycine may be similar to those seen when GABA transmissions are antagonized.