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GLYCINE
CAS NO: 56-40-6
EC/LIST NO..: 200-272-2
Glycine (symbol Gly or G;[6] /ˈɡlaɪsiːn/) is an amino acid that has a single hydrogen atom as its side chain.
Glycine is the simplest stable amino acid (carbamic acid is unstable), with the chemical formula NH2‐CH2‐COOH.
Glycine is one of the proteinogenic amino acids.
Glycine is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG).
Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form.
For the same reason, it is the most abundant amino acid in collagen triple-helices.
Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction.
Glycine is the only achiral proteinogenic amino acid.
Glycine can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom.
Glycine is a molecule with pI of 6.7, which is similar to the pH of stacking gel.
Glycine has advantage of low mobility, hydrophobicity and it does not associate with proteins.
Glycine is a component of Tris-glycine and Tris-glycine-SDS (sodium dodecyl sulfate) running buffers for polyacrylamide gel electrophoresis.
Glycine is also a component of Towbin′s transfer buffer for Western blots.
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.
Glycine 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.
Glycine is an alpha-amino acid, a serine family amino acid and a proteinogenic amino acid.
Glycine is a conjugate base of a glycinium.
Glycine is a conjugate acid of a glycinate.
Glycine is a tautomer of a glycine zwitterion.
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.
Here are the top 9 health benefits and uses of glycine.
Glycine is an amino acid.
The body can make glycine on its own, but it is also consumed in the diet. Sources include meat, fish, dairy, and legumes.
Glycine is a building block for making proteins in the body.
Glycine is also involved in transmitting chemical signals in the brain, so there's interest in using it for schizophrenia and improving memory.
A typical diet contains about 2 grams of glycine daily.
People use glycine for schizophrenia, stroke, memory and thinking skills, insomnia, and many other purposes, but there is no good scientific evidence to support most of these uses.
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.
Glycine is an amino acid, a building block for protein.
Glycine is not considered an “essential amino acid” because the body can make it from other chemicals.
A typical diet contains about 2 grams of glycine daily.
The primary sources are protein-rich foods including meat, fish, dairy, and legumes.
Glycine is used for treating schizophrenia, stroke, benign prostatic hyperplasia (BPH), and some rare inherited metabolic disorders.
Glycine is also used to protect kidneys from the harmful side effects of certain drugs used after organ transplantation as well as the liver from harmful effects of alcohol.
Other uses include cancer prevention and memory enhancement.
Some people apply glycine directly to the skin to treat leg ulcers and heal other wounds.
Glycine (Gly), is an alpha-amino acid.
These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon).
Amino acids are organic compounds that contain amino (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid.
Glycine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins.
Glycine is found in all organisms ranging from bacteria to plants to animals.
Glycine is classified as an aliphatic, non-polar amino acid and is the simplest of all amino acids.
In humans, glycine is a nonessential amino acid, although experimental animals show reduced growth on low-glycine diets.
The average adult human ingests 3 to 5 grams of glycine daily.
Glycine is a colorless, sweet-tasting crystalline solid.
Glycine is the only achiral proteinogenic amino acid.
Glycine was discovered in 1820 by the French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid.
The name comes from the Greek word glucus or "sweet tasting".
Glycine is biosynthesized in the body from the amino acid serine, which is in turn derived from 3-phosphoglycerate.
In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme).
In addition to being synthesized from serine, glycine can also be derived from threonine, choline or hydroxyproline via inter-organ metabolism of the liver and kidneys.
Glycine is degraded via three pathways.
The predominant pathway in animals and plants is the reverse of the glycine synthase pathway.
In this context, the enzyme system involved glycine metabolism is called the glycine cleavage system.
The glycine cleavage system catalyzes the oxidative conversion of glycine into carbon dioxide and ammonia, with the remaining one-carbon unit transferred to folate as methylenetetrahydrofolate.
Glycine is the main catabolic pathway for glycine and it also contributes to one-carbon metabolism.
Patients with a deficiency of this enzyme system have increased glycine in plasma, urine, and cerebrospinal fluid (CSF) with an increased CSF:plasma glycine ratio (PMID: 16151895 ).
Glycine levels are effectively measured in plasma in both normal patients and those with inborn errors of glycine metabolism .
Nonketotic hyperglycinaemia (OMIM: 606899 ) is an autosomal recessive condition caused by deficient enzyme activity of the glycine cleavage enzyme system (EC 2.1.1.10).
The glycine cleavage enzyme system comprises four proteins: P-, T-, H- and L-proteins (EC 1.4.4.2, EC 2.1.2.10, and EC 1.8.1.4 for P-, T-, and L-proteins).
Mutations have been described in the GLDC (OMIM: 238300 ), AMT (OMIM: 238310 ), and GCSH (OMIM: 238330 ) genes encoding the P-, T-, and H-proteins respectively.
Glycine is involved in the body's production of DNA, hemoglobin, and collagen, and in the release of energy.
The principal function of glycine is as a precursor to proteins.
Most proteins incorporate only small quantities of glycine, a notable exception being collagen, which contains about 35% glycine.
In higher eukaryotes, delta-aminolevulinic acid, the key precursor to porphyrins (needed for hemoglobin and cytochromes), is biosynthesized from glycine and succinyl-CoA by the enzyme ALA synthase.
Glycine provides the central C2N subunit of all purines, which are key constituents of DNA and RNA.
Glycine is an inhibitory neurotransmitter in the central nervous system, especially in the spinal cord, brainstem, and retina.
When glycine receptors are activated, chloride enters the neuron via ionotropic receptors, causing an inhibitory postsynaptic potential (IPSP).
Glycine is a non-essential amino acid that is produced naturally by the body.
Glycine is one of 20 amino acids in the human body that synthesize proteins, and it plays a key role in the creation of several other important compounds and proteins.
Glycine, NH2CH2COOH, is an organic amino acid compound used pharmacologically as a urologic irrigating solution, in intravenous solutions, and in lower-grade qualities for industrial uses.
Glycine is also used as a sweetener, and certain pharmaceutical grade products include glycine to improve gastric absorption of the drug.
Glycine is also used as an emollient, emulsifying agent, and solubilizing agent.
Glycine is an organic compound with the formula HO2CCH2NH2.
Glycine is an amino acid and is found often in small quantites in proteins.
Glycine can be found in myoglobin and hemoglobin.
Glycine; Glycine, a sweet-tasting crystalline nonessential amino acid, C2H5NO2, that is the principal amino acid occurring in sugar cane.
Glycine is derived from the alkaline hydrolysis of gelatin and used in biochemical research and medicine.
Glycine is an amino acid.
Glycine not essential to make proteins and its 3 letter abbreviation is Gly.
Glycine structure consists of a H, COOH, and NH2 bound to CH.
Glycine is an organic compound with the formula HO2CCH2NH2.
Glycine is the simplest of the twenty amino acids.
Glycine is importanct in the synthesis of proteins, peptides, purines, etc.
Glycine is the compound with the formula HO2CCH2NH2.
Glycine is one of the 20 amino acids found in animal proteins.
Glycine three letter code is gly, its one letter code is G.
Glycine is an organic compound and one of the twenty amino acids commonly found in animal proteins.
Glycine is not essential to the human diet, since it is synthesized in the body.
Glycine is one of the 20 amino acids commonly found in animal proteins.
Glycine an inhibitory neurotransmitter in the central nervous system, especially in the spinal cord, brainstem, and retina
Glycine is an organic compound most commonly found in animal proteins.
Glycine chemical formula is HO2CCH2NH2 and its molar mass is 75.07.
In addition, glycine is usually found in the industrial material called chloroacetic acid.
Glycine, C2H5NO2, is an amino acid that appears in sugar cane.
Glycine is sweet-tasting, and gotten from the alkaline hydrolysis of gelatin.
Glycine is used as a sweetener and medicine.
Glysine is an organic compound that can be obtained via hydrolysis of proteins.
Glycine is known to be a sweet tasting amino acid that can be synthesized by the human body.
Glycine is a nonessential and the simplest kind of amino acid.
Glycine is found in protein and has a sweet taste.
Glycine is used to reduce the bitter aftertaste of saccharin.
Glycine an organic compound that is usually found in animal proteins as one of the twenty amino acids.
Glycine is also used as a treatment of chloroacetic acid with ammonia.
Glycine; Glycine is an organic compound with the formula HO2CCH2NH2.
Glycine is one of the amino acids found in animal proteins, but only a small portion.
Glycine is an amino acid produced by the body that is essential to the production of collagen in bones, skin, muscles, and connective tissues.
Glycine also plays a role in nerve signal transmission and the clearance of toxins from the body.
Unlike some amino acids that are obtained solely through foods, glycine can be produced by the body.
Still, glycine can be found in high-protein foods like meat, poultry, fish, eggs, dairy, beans, cereals, and pasta.
Because of its many functions in the body, glycine is thought to offer health benefits if taken in supplement form.
This includes the treatment or prevention of insomnia, diabetes, stroke, and even certain psychiatric disorders.
Glycine is a non-chiral amino acid.
Glycine is a molecule with pI of 6.7, which is similar to the pH of stacking region in polyacrylamide gels.
Glycine has advantage of low mobility, hydrophobicity and it does not associate with proteins.
Glycine has been added in the transfer buffer during western blotting procedure.
Glycine has been used in the solution prepared for dissolving formazan crystals in the MTT (3-[4,5-dimethylthiazol-2-yl]-2,5 diphenyltetrazolium bromide) cytotoxicity assay.
Glycine has been used for terminating the rat basophilic leukemia (RBL) assay.
Glycine is the smallest of the amino acids.
Glycine is ambivalent, meaning that it can be inside or outside of the protein molecule.
In aqueous solution at or near neutral pH, glycine will exist predominantly as the zwitterion
The isoelectric point or isoelectric pH of glycine will be centered between the pKas of the two ionizable groups, the amino group and the carboxylic acid group.
In estimating the pKa of a functional group, it is important to consider the molecule as a whole.
For example, glycine is a derivative of acetic acid, and the pKa of acetic acid is well known.
Alternatively, glycine could be considered a derivative of aminoethane.
Glycine is the smallest possible of the 20 amino acids that are essential for human life.
In a seeming contradiction, glycine is called a “nonessential” amino acid because it can be synthesized by the body and therefore does not have to be included in the diet.
Glycine is the only achiral amino acid in that the carbon atom bearing the carboxylate and amino groups is not a stereogenic center.
In 1924, Hilda Louise Kingston and Samuel Barnett Schryver at the Imperial College of Science and Technology (London) isolated glycine from the hydrolysis products of gelatin.
The following year, two laboratory syntheses of glycine were published in Organic Syntheses.
In the subsequent 30 years, additional biological sources were identified and lab syntheses developed.
Just this year, humble glycine made a big splash in the news.
Scientists at the NASA Goddard Space Center (Greenbelt, MD) found glycine in particles of the comet Wild 2 that were returned to Earth by the Stardust spacecraft.
This finding confirms some scientists’ belief that biological building blocks may have come to Earth from space, but because the molecule was glycine, the origin of chirality is still murky.
Glycine is a nonpolar amino acid.
It is the simplest of the 20 natural amino acids; its side chain is a hydrogen atom.
Because there is a second hydrogen atom at the ± carbon, glycine is not optically active.
Since glycine has such a small side chain, it can fit into many places where no other amino acid can. For example, only glycine can be the internal amino acid of a collagen helix.
Glycine is very evolutionarily stable at certain positions of some proteins (for example, in cytochrome c, myoglobin, and hemoglobin), because mutations that change it to an amino acid with a larger side chain could break the protein's structure.
Most proteins contain only small quantities of glycine.
A notable exception is collagen, which is about one-third glycine.
In 1994 a team of astronomers from the University of Illinois, led by Lewis Snyder, claimed that they had found the glycine molecules in space.
Glycine turned out that they had not.
But eight years later, in 2002 Lewis Snyder and Yi-Jehng Kuan from National Taiwan Normal University repeated the finding, this time for real.
The evidence that molecules of glycine exist in interstellar space was found when 10 spectrum lines of glycine were identified by radio telescope.
According to computer simulations and lab-based experiments, glycine was probably formed when ices containing simple organic molecules were exposed to ultraviolet light.
Before glycine, more than 130 simpler molecules were found in deep space, including sugars and ethanol.
But amino acids, sometimes called building blocks of life, are a much more interesting find.
This does not prove that life exists outside Earth, but certainly make that possibility more likely, proving that amino acids exists in outer space.
This also indirectly supports the idea of Panspermia, saying that life was brought to Earth from space.
Glycine is an inhibitory neurotransmitter in the central nervous system, especially in the spinal cord. When glycine receptors are activated, chloride ions enter the neuron and the cell undergoes a hyperpolarization.
Thus the cell tends to be in an inhibited state.
Strychnine, a drug that cause convulsions, acts by blocking these glycine receptors.
Glycine was discovered in 1820 by the French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid.
He originally called it "sugar of gelatin", but the French chemist Jean-Baptiste Boussingault showed that it contained nitrogen.
The American scientist Eben Norton Horsford, then a student of the German chemist Justus von Liebig, proposed the name "glycocoll"; however, the Swedish chemist Berzelius suggested the simpler name "glycine".
The name comes from the Greek word γλυκύς "sweet tasting" (which is also related to the prefixes glyco- and gluco-, as in glycoprotein and glucose).
In 1858, the French chemist Auguste Cahours determined that glycine was an amine of acetic acid.
Although glycine can be isolated from hydrolyzed protein, this is not used for industrial production, as it can be manufactured more conveniently by chemical synthesis.
The two main processes are amination of chloroacetic acid with ammonia, giving glycine and ammonium chloride,and the Strecker amino acid synthesis, which is the main synthetic method in the United States and Japan.
About 15 thousand tonnes are produced annually in this way.
Glycine is also cogenerated as an impurity in the synthesis of EDTA, arising from reactions of the ammonia coproduct.
Glycine functions as a bidentate ligand for many metal ions, forming amino acid complexes.
A typical complex is Cu(glycinate)2, i.e. Cu(H2NCH2CO2)2, which exists both in cis and trans isomers.
With acid chlorides, glycine converts to the amidocarboxylic acid, such as hippuric acid and acetylglycine.
With nitrous acid, one obtains glycolic acid (van Slyke determination).
With methyl iodide, the amine becomes quaternized to give trimethylglycine, a natural product:
H3N+CH2COO + 3 CH3I → (CH3)3N+CH2COO− + 3 HI
Glycine condenses with itself to give peptides, beginning with the formation of glycylglycine:
2 H3N+CH2COO− → H3N+CH2CONHCH2COO− + H2O
Pyrolysis of glycine or glycylglycine gives 2,5-diketopiperazine, the cyclic diamide.
Glycine forms esters with alcohols. They are often isolated as their hydrochloride]], e.g., glycine methyl ester hydrochloride.
Otherwise the free ester tends to convert to diketopiperazine.
As a bifunctional molecule, glycine reacts with many reagents.
These can be classified into N-centered and carboxylate-center reactions.
Density 1.161 g/cm3 (20 °C)
Melting Point 233 °C (decomposition)
pH value 5.9 - 6.4 (50 g/l, H₂O, 20 °C)
Vapor pressure 0.0000171 Pa (25 °C)
Bulk density 920 kg/m3
Solubility 250 g/l soluble
In the US, glycine is typically sold in two grades: United States Pharmacopeia (“USP”), and technical grade.
USP grade sales account for approximately 80 to 85 percent of the U.S. market for glycine.
If purity greater than the USP standard is needed, for example for intravenous injections, a more expensive pharmaceutical grade glycine can be used.
Technical grade glycine, which may or may not meet USP grade standards, is sold at a lower price for use in industrial applications, e.g., as an agent in metal complexing and finishing
Glycine is not widely used in foods for its nutritional value, except in infusions.
Instead glycine's role in food chemistry is as a flavorant.
Glycine is mildly sweet, and it counters the aftertaste of saccharine.
Glycine also has preservative properties, perhaps owing to its complexation to metal ions.
Metal glycinate complexes, e.g. copper(II) glycinate are used as supplements for animal feeds.
Chemical feedstock
Glycine is an intermediate in the synthesis of a variety of chemical products.
Glycine is used in the manufacture of the herbicides glyphosate, iprodione, glyphosine, imiprothrin, and eglinazine
Glycine is used as an intermediate of the medicine such as thiamphenicol.
Laboratory research
Glycine is a significant component of some solutions used in the SDS-PAGE method of protein analysis.
Glycine serves as a buffering agent, maintaining pH and preventing sample damage during electrophoresis.
Glycine is also used to remove protein-labeling antibodies from Western blot membranes to enable the probing of numerous proteins of interest from SDS-PAGE gel.
This allows more data to be drawn from the same specimen, increasing the reliability of the data, reducing the amount of sample processing, and number of samples required.
This process is known as stripping.
Glycine has been used for the preparation of gelatin composites scaffold.
Glycine has been used in the elution buffer to extract protein using HiTrap protein G column.
Glycine has been used in the SDS-sample, running and transfer buffers prepared for SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and western blotting.
Glycine is an amino acid that serves as a building block for certain proteins, including collagen found in the skin, ligaments, muscles, bones, and cartilage.
Glycine makes up around 35% of the collagen in the human body.
Glycine also helps regulate nerve impulses, especially in the spinal cord, the retina of the eye, and the brainstem that controls subconscious body functions like breathing and heart rate.
Glycine also binds to toxins so that they can be cleared from the body.
Glycine is thought that by supplementing the glycine already produced by the body, certain health conditions may be treated or avoided.
Most of the current research has been focused on glycine's role in the central nervous system, where it may be able to improve sleep, enhance memory, and aid in the treatment of schizophrenia.
Glycine is also believed by some to reduce brain damage following a stroke, treat an enlarged prostate, heal leg ulcers, and improve insulin sensitivity in people with diabetes.
IUPAC NAME:
2-amino-3-methylpentanoic acid
2-Aminoacetic acid
2-aminoacetic acid
2-Aminoacetic acid
2-Aminoethanoic acid
Amino acetic acid
Aminoacetic acid
aminoacetic acid
Aminoacetic acid; Glycine
SYNONYMS:
200-272-2 [EINECS]
2-Aminoacetic acid [ACD/IUPAC Name]
56-40-6 [RN]
Acetic acid, amino-
Acide aminoacetique [French] [INN]
Acido aminoacetico [Spanish] [INN]
amino-Acetic acid
Aminoacetic acid
Aminoessigsäure [German]
Aminoethanoic acid
