Glycine

Last updated

Contents

Glycine [1]
Glycine-2D-skeletal.svg
Skeletal formula of neutral glycine
Glycine-zwitterion-2D-skeletal.svg
Skeletal formula of zwitterionic glycine
Glycine-neutral-Ipttt-conformer-3D-bs-17.png
Ball-and-stick model of the gas-phase structure
Glycine-zwitterion-from-xtal-3D-bs-17.png
Ball-and-stick model of the zwitterionic solid-state structure
Glycine-neutral-Ipttt-conformer-3D-sf.png
Space-filling model of the gas-phase structure
Glycine-zwitterion-from-xtal-3D-sf.png
Space-filling model of the zwitterionic solid-state structure
Names
IUPAC name
Glycine
Systematic IUPAC name
Aminoacetic acid [2]
Other names
  • 2-Aminoethanoic acid
  • Glycocol
  • Glycic acid
  • Dicarbamic acid
Identifiers
3D model (JSmol)
AbbreviationsGly, G
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.000.248 OOjs UI icon edit-ltr-progressive.svg
EC Number
  • 200-272-2
  • 227-841-8
E number E640 (flavour enhancer)
KEGG
PubChem CID
UNII
  • InChI=1S/C2H5NH2/c3-1-2(4)5/h1,3H2,(H,4,5) Yes check.svgY
    Key: DHMQDGOQFOQNFH-UHFFFAOYSA-N Yes check.svgY
  • InChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
    Key: DHMQDGOQFOQNFH-UHFFFAOYAW
  • C(C(=O)O)N
  • Zwitterion:C(C(=O)[O-])[NH3+]
  • C(C(=O)O)N.Cl
Properties
C2H5NO2
Molar mass 75.067 g·mol−1
AppearanceWhite solid
Density 1.1607 g/cm3 [3]
Melting point 233 °C (451 °F; 506 K) (decomposition)
249.9 g/L (25 °C) [4]
Solubility soluble in pyridine
sparingly soluble in ethanol
insoluble in ether
Acidity (pKa)2.34 (carboxyl), 9.6 (amino) [5]
-40.3·10−6 cm3/mol
Pharmacology
B05CX03 ( WHO )
Hazards
Lethal dose or concentration (LD, LC):
2600 mg/kg (mouse, oral)
Supplementary data page
Glycine (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yes check.svgY  verify  (what is  Yes check.svgYX mark.svgN ?)

Glycine (symbol Gly or G; [6] /ˈɡlsn/ ) [7] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable). Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8] Glycine is integral to the formation of alpha-helices in secondary protein structure due to the "flexibility" caused by such a small R group. Glycine is also an inhibitory neurotransmitter [9] – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction. [10]

It is the only achiral proteinogenic amino acid. [11] It can fit into hydrophilic or hydrophobic environments, due to its minimal side chain of only one hydrogen atom. [12]

History and etymology

Glycine was discovered in 1820 by French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid. [13] He originally called it "sugar of gelatin", [14] [15] but French chemist Jean-Baptiste Boussingault showed in 1838 that it contained nitrogen. [16] In 1847 American scientist Eben Norton Horsford, then a student of the German chemist Justus von Liebig, proposed the name "glycocoll"; [17] [18] however, the Swedish chemist Berzelius suggested the simpler current name a year later. [19] [20] The name comes from the Greek word γλυκύς "sweet tasting" [21] (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. [22]

Production

Although glycine can be isolated from hydrolyzed proteins, this route is not used for industrial production, as it can be manufactured more conveniently by chemical synthesis. [23] The two main processes are amination of chloroacetic acid with ammonia, giving glycine and hydrochloric acid, [24] and the Strecker amino acid synthesis, [25] which is the main synthetic method in the United States and Japan. [26] About 15 thousand tonnes are produced annually in this way. [27]

Glycine is also co-generated as an impurity in the synthesis of EDTA, arising from reactions of the ammonia co-product. [28]

Chemical reactions

Its acid–base properties are most important. In aqueous solution, glycine is amphoteric: below pH = 2.4, it converts to the ammonium cation called glycinium. Above about pH 9.6, it converts to glycinate.

Glycine-protonation-states-2D-skeletal.png

Glycine functions as a bidentate ligand for many metal ions, forming amino acid complexes. [29] A typical complex is Cu(glycinate)2, i.e. Cu(H2NCH2CO2)2, which exists both in cis and trans isomers. [30] [31]

With acid chlorides, glycine converts to the amidocarboxylic acid, such as hippuric acid [32] and acetylglycine. [33] With nitrous acid, one obtains glycolic acid (van Slyke determination). With methyl iodide, the amine becomes quaternized to give trimethylglycine, a natural product:

H
3
N+
CH
2
COO
+ 3 CH3I → (CH
3
)
3
N+
CH
2
COO
+ 3 HI

Glycine condenses with itself to give peptides, beginning with the formation of glycylglycine: [34]

2 H
3
N+
CH
2
COO
H
3
N+
CH
2
CONHCH
2
COO
+ H2O

Pyrolysis of glycine or glycylglycine gives 2,5-diketopiperazine, the cyclic diamide. [35]

Glycine forms esters with alcohols. They are often isolated as their hydrochloride, such as 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.

Metabolism

Biosynthesis

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-phosphoglycerate. In most organisms, the enzyme serine hydroxymethyltransferase catalyses this transformation via the cofactor pyridoxal phosphate: [36]

serine + tetrahydrofolate → glycine + N5,N10-methylene tetrahydrofolate + H2O

In E. coli, glycine is sensitive to antibiotics that target folate. [37]

In the liver of vertebrates, glycine synthesis is catalyzed by glycine synthase (also called glycine cleavage enzyme). This conversion is readily reversible: [36]

CO2 + NH+
4
+ N5,N10-methylene tetrahydrofolate + NADH + H+ ⇌ Glycine + tetrahydrofolate + NAD +

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. [38]

Degradation

Glycine is degraded via three pathways. The predominant pathway in animals and plants is the reverse of the glycine synthase pathway mentioned above. In this context, the enzyme system involved is usually called the glycine cleavage system: [36]

Glycine + tetrahydrofolate + NAD+ ⇌ CO2 + NH+
4
+ N5,N10-methylene tetrahydrofolate + 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. [36]

In the third pathway of its 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. [36]

The half-life of glycine and its elimination from the body varies significantly based on dose. [39] In one study, the half-life varied between 0.5 and 4.0 hours. [39]

Physiological function

The principal function of glycine is it acts as a precursor to proteins. Most proteins incorporate only small quantities of glycine, a notable exception being collagen, which contains about 35% glycine due to its periodically repeated role in the formation of collagen's helix structure in conjunction with hydroxyproline. [36] [40] In the genetic code, glycine is coded by all codons starting with GG, namely GGU, GGC, GGA and GGG. [8]

As a biosynthetic intermediate

In higher eukaryotes, δ-aminolevulinic acid, the key precursor to porphyrins, is biosynthesized from glycine and succinyl-CoA by the enzyme ALA synthase. Glycine provides the central C2N subunit of all purines. [36]

As a neurotransmitter

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). Strychnine is a strong antagonist at ionotropic glycine receptors, whereas bicuculline is a weak one. Glycine is a required co-agonist along with glutamate for NMDA receptors. In contrast to the inhibitory role of glycine in the spinal cord, this behaviour is facilitated at the (NMDA) glutamatergic receptors which are excitatory. [41] The LD50 of glycine is 7930 mg/kg in rats (oral), [42] and it usually causes death by hyperexcitability.

As a toxin conjugation agent

Glycine conjugation pathway has not been fully investigated. [43] Glycine is thought to be a hepatic detoxifier of a number endogenous and xenobiotic organic acids. [44] Bile acids are normally conjugated to glycine in order to increase their solubility in water. [45]

The human body rapidly clears sodium benzoate by combining it with glycine to form hippuric acid which is then excreted. [46] The metabolic pathway for this begins with the conversion of benzoate by butyrate-CoA ligase into an intermediate product, benzoyl-CoA, [47] which is then metabolized by glycine N-acyltransferase into hippuric acid. [48]

Uses

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. [49]

Animal and human foods

Structure of cis-Cu(glycinate)2(H2O) Cu(gly)2(OH2).png
Structure of cis-Cu(glycinate)2(H2O)

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. It is mildly sweet, and it counters the aftertaste of saccharine. It 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. [27]

As of 1971, the U.S. Food and Drug Administration "no longer regards glycine and its salts as generally recognized as safe for use in human food", [51] and only permits food uses of glycine in certain conditions. [52]

Glycine has been researched for its potential to extend life. [53] [54] The proposed mechanisms of this effect are its ability to clear methionine from the body, and activating autophagy. [53]

Chemical feedstock

Glycine is an intermediate in the synthesis of a variety of chemical products. It is used in the manufacture of the herbicides glyphosate, [55] iprodione, glyphosine, imiprothrin, and eglinazine. [27] It is used as an intermediate of antibiotics such as thiamphenicol.[ citation needed ]

Laboratory research

Glycine is a significant component of some solutions used in the SDS-PAGE method of protein analysis. It serves as a buffering agent, maintaining pH and preventing sample damage during electrophoresis. [56] 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. [57] This process is known as stripping.

Presence in space

The presence of glycine outside the Earth was confirmed in 2009, based on the analysis of samples that had been taken in 2004 by the NASA spacecraft Stardust from comet Wild 2 and subsequently returned to Earth. Glycine had previously been identified in the Murchison meteorite in 1970. [58] The discovery of glycine in outer space bolstered the hypothesis of so-called soft-panspermia, which claims that the "building blocks" of life are widespread throughout the universe. [59] In 2016, detection of glycine within Comet 67P/Churyumov–Gerasimenko by the Rosetta spacecraft was announced. [60]

The detection of glycine outside the Solar System in the interstellar medium has been debated. [61]

Evolution

Glycine is proposed to be defined by early genetic codes. [62] [63] [64] [65] For example, low complexity regions (in proteins), that may resemble the proto-peptides of the early genetic code are highly enriched in glycine. [65]

Presence in foods

Food sources of glycine [66]
FoodPercentage
content
by weight
(g/100g)
Snacks, pork skins 11.04
Sesame seeds flour (low fat)3.43
Beverages, protein powder (soy-based)2.37
Seeds, safflower seed meal, partially defatted2.22
Meat, bison, beef and others (various parts)1.5–2.0
Gelatin desserts1.96
Seeds, pumpkin and squash seed kernels1.82
Turkey, all classes, back, meat and skin1.79
Chicken, broilers or fryers, meat and skin1.74
Pork, ground, 96% lean / 4% fat, cooked, crumbles1.71
Bacon and beef sticks1.64
Peanuts 1.63
Crustaceans, spiny lobster1.59
Spices, mustard seed, ground1.59
Salami 1.55
Nuts, butternuts, dried1.51
Fish, salmon, pink, canned, drained solids1.42
Almonds 1.42
Fish, mackerel 0.93
Cereals ready-to-eat, granola, homemade0.81
Leeks, (bulb and lower-leaf portion), freeze-dried0.7
Cheese, parmesan (and others), grated0.56
Soybeans, green, cooked, boiled, drained, without salt0.51
Bread, protein (includes gluten)0.47
Egg, whole, cooked, fried0.47
Beans, white, mature seeds, cooked, boiled, with salt0.38
Lentils, mature seeds, cooked, boiled, with salt0.37

See also

Related Research Articles

<span class="mw-page-title-main">Amino acid</span> Organic compounds containing amine and carboxylic groups

Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.

<span class="mw-page-title-main">Phenylalanine</span> Type of α-amino acid

Phenylalanine is an essential α-amino acid with the formula C
9
H
11
NO
2
. It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine. This essential amino acid is classified as neutral, and nonpolar because of the inert and hydrophobic nature of the benzyl side chain. The L-isomer is used to biochemically form proteins coded for by DNA. Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the biological pigment melanin. It is encoded by the messenger RNA codons UUU and UUC.

Serine is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC.

<span class="mw-page-title-main">Threonine</span> Amino acid

Threonine is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, 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.

<span class="mw-page-title-main">NMDA receptor</span> Glutamate receptor and ion channel protein found in nerve cells

The N-methyl-D-aspartatereceptor (also known as the NMDA receptor or NMDAR), is a glutamate receptor and predominantly Ca2+ ion channel found in neurons. The NMDA receptor is one of three types of ionotropic glutamate receptors, the other two being AMPA and kainate receptors. Depending on its subunit composition, its ligands are glutamate and glycine (or D-serine). However, the binding of the ligands is typically not sufficient to open the channel as it may be blocked by Mg2+ ions which are only removed when the neuron is sufficiently depolarized. Thus, the channel acts as a "coincidence detector" and only once both of these conditions are met, the channel opens and it allows positively charged ions (cations) to flow through the cell membrane. The NMDA receptor is thought to be very important for controlling synaptic plasticity and mediating learning and memory functions.

<span class="mw-page-title-main">Sarcosine</span> Chemical compound

Sarcosine, also known as N-methylglycine, or monomethylglycine, is a amino acid 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.

β-Alanine Chemical compound

β-Alanine (beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is attached to the β-carbon instead of the more usual α-carbon for alanine (α-alanine). The IUPAC name for β-alanine is 3-aminopropanoic acid. Unlike its counterpart α-alanine, β-alanine has no stereocenter.

Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients serve as enzyme substrates, with conversion by the living organism either into simpler or more complex products. Examples of biosynthetic pathways include those for the production of amino acids, lipid membrane components, and nucleotides, but also for the production of all classes of biological macromolecules, and of acetyl-coenzyme A, adenosine triphosphate, nicotinamide adenine dinucleotide and other key intermediate and transactional molecules needed for metabolism. Thus, in biosynthesis, any of an array of compounds, from simple to complex, are converted into other compounds, and so it includes both the catabolism and anabolism of complex molecules. Biosynthetic processes are often represented via charts of metabolic pathways. A particular biosynthetic pathway may be located within a single cellular organelle, while others involve enzymes that are located across an array of cellular organelles and structures.

<span class="mw-page-title-main">Ligand-gated ion channel</span> Type of ion channel transmembrane protein

Ligand-gated ion channels (LICs, LGIC), also commonly referred to as ionotropic receptors, are a group of transmembrane ion-channel proteins which open to allow ions such as Na+, K+, Ca2+, and/or Cl to pass through the membrane in response to the binding of a chemical messenger (i.e. a ligand), such as a neurotransmitter.

<span class="mw-page-title-main">Hippuric acid</span> Chemical compound

Hippuric acid is a carboxylic acid and organic compound. It is found in urine and is formed from the combination of benzoic acid and glycine. Levels of hippuric acid rise with the consumption of phenolic compounds. The phenols are first converted to benzoic acid, and then to hippuric acid and excreted in urine.

<span class="mw-page-title-main">Glycolic acid</span> Chemical compound

Glycolic acid is a colorless, odorless and hygroscopic crystalline solid, highly soluble in water. It is used in various skin-care products. Glycolic acid is widespread in nature. A glycolate is a salt or ester of glycolic acid.

<span class="mw-page-title-main">PDZ domain</span>

The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses and animals. Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes. PDZ domains also play a highly significant role in the anchoring of cell surface receptors to the actin cytoskeleton via mediators like NHERF and ezrin.

<span class="mw-page-title-main">D-amino acid oxidase</span> Enzyme

D-amino acid oxidase is an enzyme with the function on a molecular level to oxidize D-amino acids to the corresponding α-keto acids, producing ammonia and hydrogen peroxide. This results in a number of physiological effects in various systems, most notably the brain. The enzyme is most active toward neutral D-amino acids, and not active toward acidic D-amino acids. One of its most important targets in mammals is D-Serine in the central nervous system. By targeting this and other D-amino acids in vertebrates, DAAO is important in detoxification. The role in microorganisms is slightly different, breaking down D-amino acids to generate energy.

<span class="mw-page-title-main">Kynurenic acid</span> Chemical compound

Kynurenic acid is a product of the normal metabolism of amino acid L-tryptophan. It has been shown that kynurenic acid possesses neuroactive activity. It acts as an antiexcitotoxic and anticonvulsant, most likely through acting as an antagonist at excitatory amino acid receptors. Because of this activity, it may influence important neurophysiological and neuropathological processes. As a result, kynurenic acid has been considered for use in therapy in certain neurobiological disorders. Conversely, increased levels of kynurenic acid have also been linked to certain pathological conditions.

<span class="mw-page-title-main">Quisqualic acid</span> Chemical compound

Quisqualic acid is an agonist of the AMPA, kainate, and group I metabotropic glutamate receptors. It is one of the most potent AMPA receptor agonists known. It causes excitotoxicity and is used in neuroscience to selectively destroy neurons in the brain or spinal cord. Quisqualic acid occurs naturally in the seeds of Quisqualis species.

<span class="mw-page-title-main">Serine hydroxymethyltransferase</span> InterPro Family

Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-methylenetetrahydrofolate (5,10-CH2-THF). This reaction provides the largest part of the one-carbon units available to the cell.

<span class="mw-page-title-main">GCSH</span> Protein-coding gene in the species Homo sapiens

Glycine cleavage system H protein, mitochondrial is a protein that in humans is encoded by the GCSH gene. Degradation of glycine is brought about by the glycine cleavage system (GCS), which is composed of 4 protein components: P protein, H protein, T protein, and L protein. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. The protein encoded by GCSH gene is the H protein, which transfers the methylamine group of glycine from the P protein to the T protein. Defects in this gene are a cause of nonketotic hyperglycinemia (NKH). Two transcript variants, one protein-coding and the other probably not protein-coding, have been found for this gene. Also, several transcribed and non-transcribed pseudogenes of this gene exist throughout the genome.

<span class="mw-page-title-main">Glycine cleavage system</span> Enzymes that break down glycine

The glycine cleavage system (GCS) is also known as the glycine decarboxylase complex or GDC. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine. The same set of enzymes is sometimes referred to as glycine synthase when it runs in the reverse direction to form glycine. The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex, so it is more appropriate to call it a "system" instead of a "complex". The H-protein is responsible for interacting with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both animals and plants, the glycine cleavage system is loosely attached to the inner membrane of the mitochondria. Mutations in this enzymatic system are linked with glycine encephalopathy.

<i>N</i>-Arachidonylglycine Chemical compound

N-Arachidonylglycine (NAGly) is a carboxylic metabolite of the endocannabinoid anandamide (AEA). Since it was first synthesized in 1996, NAGly has been a primary focus of the relatively contemporary field of lipidomics due to its wide range of signaling targets in the brain, the immune system and throughout various other bodily systems. In combination with 2‐arachidonoyl glycerol (2‐AG), NAGly has enabled the identification of a family of lipids often referred to as endocannabinoids. Recently, NAGly has been found to bind to G-protein coupled receptor 18 (GPR18), the putative abnormal cannabidiol receptor. NaGly is an endogenous inhibitor of fatty acid amide hydrolase (FAAH) and thereby increases the ethanolamide endocannabinoids AEA, oleoylethanolamide (OEA) and palmitoylethanolamide (PEA) levels. NaGly is found throughout the body and research on its explicit functions is ongoing.

mTORC1 Protein complex

mTORC1, also known as mammalian target of rapamycin complex 1 or mechanistic target of rapamycin complex 1, is a protein complex that functions as a nutrient/energy/redox sensor and controls protein synthesis.

References

  1. The Merck Index: An Encyclopedia of Chemicals, Drugs, and Biologicals (11th ed.). Merck. 1989. ISBN   091191028X.,4386
  2. "Glycine". PubChem.
  3. Handbook of Chemistry and Physics, CRC Press, 59th edition, 1978.[ page needed ]
  4. "Solubilities and densities". Prowl.rockefeller.edu. Archived from the original on September 12, 2017. Retrieved November 13, 2013.
  5. Dawson, R.M.C., et al., Data for Biochemical Research, Oxford, Clarendon Press, 1959.[ page needed ]
  6. "Nomenclature and Symbolism for Amino Acids and Peptides". IUPAC-IUB Joint Commission on Biochemical Nomenclature. 1983. Archived from the original on October 9, 2008. Retrieved March 5, 2018.
  7. "Glycine | Definition of glycine in English by Oxford Dictionaries". Archived from the original on January 29, 2018.
  8. 1 2 Pawlak K, Błażej P, Mackiewicz D, Mackiewicz P (January 2023). "The Influence of the Selection at the Amino Acid Level on Synonymous Codon Usage from the Viewpoint of Alternative Genetic Codes". International Journal of Molecular Sciences. 24 (2): 1185. doi: 10.3390/ijms24021185 . PMC   9866869 . PMID   36674703.
  9. Zafra F, Aragón C, Giménez C (June 1997). "Molecular biology of glycinergic neurotransmission". Molecular Neurobiology. 14 (3): 117–142. doi:10.1007/BF02740653. PMID   9294860.
  10. Atchison W (2018). "Toxicology of the Neuromuscular Junction". Comprehensive Toxicology. pp. 259–282. doi:10.1016/B978-0-12-801238-3.99198-0. ISBN   978-0-08-100601-6.
  11. Matsumoto A, Ozaki H, Tsuchiya S, Asahi T, Lahav M, Kawasaki T, et al. (April 2019). "Achiral amino acid glycine acts as an origin of homochirality in asymmetric autocatalysis". Organic & Biomolecular Chemistry. 17 (17): 4200–4203. doi:10.1039/C9OB00345B. PMID   30932119.
  12. Alves A, Bassot A, Bulteau AL, Pirola L, Morio B (June 2019). "Glycine Metabolism and Its Alterations in Obesity and Metabolic Diseases". Nutrients. 11 (6): 1356. doi: 10.3390/nu11061356 . PMC   6627940 . PMID   31208147.
  13. Plimmer RH (1912) [1908]. Plimmer RH, Hopkins F (eds.). The chemical composition of the proteins. Monographs on biochemistry. Vol. Part I. Analysis (2nd ed.). London: Longmans, Green and Co. p. 82. Retrieved January 18, 2010.
  14. Braconnot H (1820). "Sur la conversion des matières animales en nouvelles substances par le moyen de l'acide sulfurique" [On the conversion of animal materials into new substances by means of sulfuric acid]. Annales de Chimie et de Physique. 2nd series (in French). 13: 113–125. ; see p. 114.
  15. MacKenzie C (1822). One Thousand Experiments in Chemistry: With Illustrations of Natural Phenomena; and Practical Observations on the Manufacturing and Chemical Processes at Present Pursued in the Successful Cultivation of the Useful Arts ... Sir R. Phillips and Company. p.  557.
  16. Boussingault (1838). "Sur la composition du sucre de gélatine et de l'acide nitro-saccharique de Braconnot" [On the composition of sugar of gelatine and of nitro-glucaric acid of Braconnot]. Comptes Rendus (in French). 7: 493–495.
  17. Horsford EN (1847). "Glycocoll (gelatine sugar) and some of its products of decomposition". The American Journal of Science and Arts. 2nd series. 3: 369–381.
  18. Ihde AJ (1984). The Development of Modern Chemistry. Courier Corporation. p. 167. ISBN   978-0-486-64235-2.
  19. Berzelius J (1848). Jahres-Bericht über die Fortschritte der Chemie und Mineralogie (Annual Report on the Progress of Chemistry and Mineralogy). Vol. 47. Tübigen, (Germany): Laupp. p. 654. From p. 654: "Er hat dem Leimzucker als Basis den Namen Glycocoll gegeben. ... Glycin genannt werden, und diesen Namen werde ich anwenden." (He [i.e., the American scientist Eben Norton Horsford, then a student of the German chemist Justus von Liebig] gave the name "glycocoll" to Leimzucker [sugar of gelatine], a base. This name is not euphonious and has besides the flaw that it clashes with the names of the rest of the bases. It is compounded from γλυχυς (sweet) and χολλα (animal glue). Since this organic base is the only [one] which tastes sweet, then it can much more briefly be named "glycine", and I will use this name.)
  20. Nye MJ (1999). Before Big Science: The Pursuit of Modern Chemistry and Physics, 1800-1940. Harvard University Press. p. 141. ISBN   978-0-674-06382-2.
  21. "glycine". Oxford Dictionaries. Archived from the original on November 13, 2014. Retrieved December 6, 2015.
  22. Cahours A (1858). "Recherches sur les acides amidés" [Investigations into aminated acids]. Comptes Rendus (in French). 46: 1044–1047.
  23. Okafor N (2016). Modern Industrial Microbiology and Biotechnology. CRC Press. p. 385. ISBN   978-1-4398-4323-9.
  24. Ingersoll AW, Babcock SH (1932). "Hippuric acid". Organic Syntheses . 12: 40; Collected Volumes, vol. 2, p. 328.
  25. Kirk-Othmer Food and Feed Technology, 2 Volume Set. John Wiley & Sons. 2007. p. 38. ISBN   978-0-470-17448-7.
  26. "Glycine Conference (prelim)". USITC. Archived from the original on February 22, 2012. Retrieved June 13, 2014.{{cite web}}: CS1 maint: bot: original URL status unknown (link)
  27. 1 2 3 Drauz K, Grayson I, Kleemann A, Krimmer HP, Leuchtenberger W, Weckbecker C (2007). "Amino Acids". Ullmann's Encyclopedia of Industrial Chemistry. doi:10.1002/14356007.a02_057.pub2. ISBN   978-3-527-30385-4.
  28. Hart JR (2005). "Ethylenediaminetetraacetic Acid and Related Chelating Agents". Ullmann's Encyclopedia of Industrial Chemistry . Weinheim: Wiley-VCH. doi:10.1002/14356007.a10_095. ISBN   978-3527306732.
  29. Tomiyasu H, Gordon G (April 1976). "Ring closure in the reaction of metal chelates. Formation of the bidentate oxovanadium(IV)-glycine complex". Inorganic Chemistry. 15 (4): 870–874. doi:10.1021/ic50158a027.
  30. Lutz OM, Messner CB, Hofer TS, Glätzle M, Huck CW, Bonn GK, et al. (May 2013). "Combined Ab Initio Computational and Infrared Spectroscopic Study of the cis- and trans-Bis(glycinato)copper(II) Complexes in Aqueous Environment". The Journal of Physical Chemistry Letters. 4 (9): 1502–1506. doi:10.1021/jz400288c. PMID   26282305.
  31. D'Angelo P, Bottari E, Festa MR, Nolting HF, Pavel NV (April 1998). "X-ray Absorption Study of Copper(II)−Glycinate Complexes in Aqueous Solution". The Journal of Physical Chemistry B. 102 (17): 3114–3122. doi:10.1021/jp973476m.
  32. Ingersoll AW, Babcock SH (1932). "Hippuric Acid". Org. Synth. 12: 40. doi:10.15227/orgsyn.012.0040.
  33. Herbst RM, Shemin D (1939). "Acetylglycine". Org. Synth. 19: 4. doi:10.15227/orgsyn.019.0004.
  34. Van Dornshuld E, Vergenz RA, Tschumper GS (July 2014). "Peptide bond formation via glycine condensation in the gas phase". The Journal of Physical Chemistry B. 118 (29): 8583–8590. doi:10.1021/jp504924c. PMID   24992687.
  35. Leng L, Yang L, Zu H, Yang J, Ai Z, Zhang W, et al. (November 2023). "Insights into glycine pyrolysis mechanisms: Integrated experimental and molecular dynamics/DFT simulation studies". Fuel. 351: 128949. Bibcode:2023Fuel..35128949L. doi:10.1016/j.fuel.2023.128949.
  36. 1 2 3 4 5 6 7 Nelson DL, Cox MM (2005). Principles of Biochemistry (4th ed.). New York: W. H. Freeman. pp. 127, 675–77, 844, 854. ISBN   0-7167-4339-6.
  37. Kwon YK, Higgins MB, Rabinowitz JD (August 2010). "Antifolate-induced depletion of intracellular glycine and purines inhibits thymineless death in E. coli". ACS Chemical Biology. 5 (8): 787–795. doi:10.1021/cb100096f. PMC   2945287 . PMID   20553049.
  38. Wang W, Wu Z, Dai Z, Yang Y, Wang J, Wu G (September 2013). "Glycine metabolism in animals and humans: implications for nutrition and health". Amino Acids. 45 (3): 463–477. doi:10.1007/s00726-013-1493-1. PMID   23615880. S2CID   7577607.
  39. 1 2 Hahn RG (1993). "Dose-dependent half-life of glycine". Urological Research. 21 (4): 289–291. doi:10.1007/BF00307714. PMID   8212419. S2CID   25138444.
  40. Szpak P (2011). "Fish bone chemistry and ultrastructure: implications for taphonomy and stable isotope analysis". Journal of Archaeological Science . 38 (12): 3358–3372. Bibcode:2011JArSc..38.3358S. doi:10.1016/j.jas.2011.07.022.
  41. Liu Y, Zhang J (October 2000). "Recent development in NMDA receptors". Chinese Medical Journal. 113 (10): 948–56. PMID   11775847.
  42. "Safety (MSDS) data for glycine". The Physical and Theoretical Chemistry Laboratory Oxford University. 2005. Archived from the original on October 20, 2007. Retrieved November 1, 2006.
  43. van der Sluis R, Badenhorst CP, Erasmus E, van Dyk E, van der Westhuizen FH, van Dijk AA (October 2015). "Conservation of the coding regions of the glycine N-acyltransferase gene further suggests that glycine conjugation is an essential detoxification pathway". Gene. 571 (1): 126–134. doi:10.1016/j.gene.2015.06.081. PMID   26149650.
  44. Badenhorst CP, Erasmus E, van der Sluis R, Nortje C, van Dijk AA (August 2014). "A new perspective on the importance of glycine conjugation in the metabolism of aromatic acids". Drug Metabolism Reviews. 46 (3): 343–361. doi:10.3109/03602532.2014.908903. PMID   24754494.
  45. Di Ciaula A, Garruti G, Lunardi Baccetto R, Molina-Molina E, Bonfrate L, Wang DQ, et al. (November 2017). "Bile Acid Physiology". Annals of Hepatology. 16 (Suppl. 1: s3-105): s4–s14. doi: 10.5604/01.3001.0010.5493 . hdl: 11586/203563 . PMID   29080336.
  46. Nair B (January 2001). "Final report on the safety assessment of Benzyl Alcohol, Benzoic Acid, and Sodium Benzoate". International Journal of Toxicology. 20 Suppl 3 (3_suppl): 23–50. doi:10.1080/10915810152630729. PMID   11766131.
  47. "butyrate-CoA ligase". BRENDA. Technische Universität Braunschweig. Retrieved May 7, 2014. Substrate/Product
  48. "glycine N-acyltransferase". BRENDA. Technische Universität Braunschweig. Retrieved May 7, 2014. Substrate/Product
  49. "Glycine From Japan and Korea" (PDF). U.S. International Trade Commission. January 2008. Archived (PDF) from the original on June 6, 2010. Retrieved June 13, 2014.
  50. Casari BM, Mahmoudkhani AH, Langer V (2004). "A Redetermination of cis-Aquabis(glycinato-κ2N,O)copper(II)". Acta Crystallogr. E. 60 (12): m1949–m1951. doi:10.1107/S1600536804030041.
  51. "eCFR :: 21 CFR 170.50 -- Glycine (aminoacetic acid) in food for human consumption". ecfr.gov. Retrieved October 24, 2022.
  52. "eCFR :: 21 CFR 172.812 -- Glycine". ecfr.gov. Retrieved July 6, 2024.
  53. 1 2 Johnson AA, Cuellar TL (June 2023). "Glycine and aging: Evidence and mechanisms". Ageing Research Reviews. 87: 101922. doi: 10.1016/j.arr.2023.101922 . PMID   37004845.
  54. Soh J, Raventhiran S, Lee JH, Lim ZX, Goh J, Kennedy BK, et al. (February 2024). "The effect of glycine administration on the characteristics of physiological systems in human adults: A systematic review". GeroScience. 46 (1): 219–239. doi:10.1007/s11357-023-00970-8. PMC   10828290 . PMID   37851316.
  55. Stahl SS, Alsters PL (2016). Liquid Phase Aerobic Oxidation Catalysis: Industrial Applications and Academic Perspectives. John Wiley & Sons. p. 268. ISBN   978-3-527-69015-2.
  56. Schägger H (May 12, 2006). "Tricine-SDS-PAGE". Nature Protocols. 1 (1): 16–22. doi:10.1038/nprot.2006.4. PMID   17406207.
  57. Legocki RP, Verma DP (March 1981). "Multiple immunoreplica Technique: screening for specific proteins with a series of different antibodies using one polyacrylamide gel". Analytical Biochemistry. 111 (2): 385–392. doi:10.1016/0003-2697(81)90577-7. PMID   6166216.
  58. Kvenvolden K, Lawless J, Pering K, Peterson E, Flores J, Ponnamperuma C, et al. (December 1970). "Evidence for extraterrestrial amino-acids and hydrocarbons in the Murchison meteorite". Nature. 228 (5275): 923–926. Bibcode:1970Natur.228..923K. doi:10.1038/228923a0. PMID   5482102. S2CID   4147981.
  59. "Building block of life found on comet - Thomson Reuters 2009". Reuters. August 18, 2009. Retrieved August 18, 2009.
  60. European Space Agency (May 27, 2016). "Rosetta's comet contains ingredients for life" . Retrieved June 5, 2016.
  61. Ramos MF, Silva NA, Muga NJ, Pinto AN (February 2020). "Reversal operator to compensate polarization random drifts in quantum communications". Optics Express. 28 (4): 5035–5049. arXiv: astro-ph/0410335 . Bibcode:2005ApJ...619..914S. doi:10.1086/426677. PMID   32121732. S2CID   16286204.
  62. Trifonov EN (December 2000). "Consensus temporal order of amino acids and evolution of the triplet code". Gene. 261 (1): 139–151. doi:10.1016/S0378-1119(00)00476-5. PMID   11164045.
  63. Higgs PG, Pudritz RE (June 2009). "A thermodynamic basis for prebiotic amino acid synthesis and the nature of the first genetic code". Astrobiology. 9 (5): 483–490. arXiv: 0904.0402 . Bibcode:2009AsBio...9..483H. doi:10.1089/ast.2008.0280. PMID   19566427. S2CID   9039622 .
  64. Chaliotis A, Vlastaridis P, Mossialos D, Ibba M, Becker HD, Stathopoulos C, et al. (February 2017). "The complex evolutionary history of aminoacyl-tRNA synthetases". Nucleic Acids Research. 45 (3): 1059–1068. doi: 10.1093/nar/gkw1182 . PMC   5388404 . PMID   28180287.
  65. 1 2 Ntountoumi C, Vlastaridis P, Mossialos D, Stathopoulos C, Iliopoulos I, Promponas V, et al. (November 2019). "Low complexity regions in the proteins of prokaryotes perform important functional roles and are highly conserved". Nucleic Acids Research. 47 (19): 9998–10009. doi: 10.1093/nar/gkz730 . PMC   6821194 . PMID   31504783.
  66. "FoodData Central Search Results for "Glycine (g)"". fdc.nal.usda.gov. Retrieved May 26, 2024.

Further reading