Alanine Identifiers CAS number , (L-isomer), (racemic)(D-isomer) PubChem ChemSpider , (L-isomer), (Racemic)(D-isomer) UNII EC-number KEGG ChEBI ChEMBL IUPHAR ligand Jmol-3D images Image 1
Properties Molecular formula C3H7NO2 Molar mass 89.09 g mol−1 Appearance white powder Density 1.424 g/cm3 Melting point
258 °C, 531 K, 496 °F (subl.)
Solubility in water 167.2 g/L (25 °C) Acidity (pKa) 2.35 (carboxyl), 9.69 (amino) Supplementary data page Structure and
n, εr, etc. Thermodynamic
Solid, liquid, gas
Spectral data UV, IR, NMR, MS (what is: /?)
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Alanine (abbreviated as Ala or A) is an α-amino acid with the chemical formula CH3CH(NH2)COOH. The L-isomer is one of the 20 amino acids encoded by the genetic code. Its codons are GCU, GCC, GCA, and GCG. It is classified as a nonpolar amino acid. L-Alanine is second only to leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins. D-Alanine occurs in bacterial cell walls and in some peptide antibiotics.
The α-carbon atom of alanine is bound with a methyl group (-CH3), making it one of the simplest α-amino acids with respect to molecular structure and also resulting in alanine's being classified as an aliphatic amino acid. The methyl group of alanine is non-reactive and is thus almost never directly involved in protein function.
Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained directly through the diet. Alanine is found in a wide variety of foods, but is particularly concentrated in meats.
Good sources of alanine include
- Animal sources: meat, seafood, caseinate, dairy products, eggs, fish, gelatin, lactalbumin
- Vegetarian sources: beans, nuts, seeds, soy, whey, brewer's yeast, brown rice, bran, corn, legumes, whole grains.
Alanine is most commonly produced by reductive amination of pyruvate. Because transamination reactions are readily reversible and pyruvate pervasive, alanine can be easily formed and thus has close links to metabolic pathways such as glycolysis, gluconeogenesis, and the citric acid cycle. It also arises together with lactate and generates glucose from protein via the alanine cycle.
Racemic alanine can be prepared by the condensation of acetaldehyde with ammonium chloride in the presence of sodium cyanide by the Strecker reaction, or by the ammonolysis of 2-bromopropanoic acid:
Alanine plays a key role in glucose–alanine cycle between tissues and liver. In muscle and other tissues that degrade amino acids for fuel, amino groups are collected in the form of glutamate by transamination. Glutamate can then transfer its amino group through the action of alanine aminotransferase to pyruvate, a product of muscle glycolysis, forming alanine and α-ketoglutarate. The alanine formed is passed into the blood and transported to the liver. A reverse of the alanine aminotransferase reaction takes place in liver. Pyruvate regenerated forms glucose through gluconeogenesis, which returns to muscle through the circulation system. Glutamate in the liver enters mitochondria and degrades into ammonium ion through the action of glutamate dehydrogenase, which in turn participate in the urea cycle to form urea.
The glucose–alanine cycle enables pyruvate and glutamate to be removed from the muscle and find their way to the liver. Glucose is regenerated from pyruvate and then returned to muscle: the energetic burden of gluconeogenesis is thus imposed on the liver instead of the muscle. All available ATP in muscle is devoted to muscle contraction.
Link to hypertension
Link to Diabetes
Alterations in the alanine cycle that increase the levels of serum alanine aminotransferase (ALT) is linked to the development of diabetes. With an elevated level of ALT the risk of developing diabetes increases.
Free radical stability
This property of alanine is used in dosimetric measurements in radiotherapy. When normal alanine is irradiated, the radiation causes certain alanine molecules to become free radicals, and, as these radicals are stable, the free radical content can later be measured in order to find out how much radiation the alanine was exposed to. In this way, one can be assured that complex radiotherapy treatment plans will deliver the intended pattern of radiation dose.
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- ^ Kendall, E. C.; McKenzie, B. F. (1929), "dl-Alanine", Org. Synth. 9: 4, http://www.orgsyn.org/orgsyn/orgsyn/prepContent.asp?prep=cv1p0021 ; Coll. Vol. 1: 21 .
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- ^ Highfield, Roger (2008-04-21), "'Metabolic fingerprint' linked to high blood pressure", Daily Telegraph, http://www.telegraph.co.uk/earth/main.jhtml?view=DETAILS&grid=&xml=/earth/2008/04/21/sciblood121.xml .
- ^ "Elevated Alanine Aminotransferase Predicts New-Onset Type 2 Diabetes Independently of Classical Risk Factors, Metabolic Syndrome, and C-Reactive Protein in the West of Scotland Coronary Prevention Study". http://www.medscape.com/viewarticle/492759.
- ^ Zagórski, Z. P.; Sehested, K. (1998), "Transients and stable radical from the deamination of α-alanine", J. Radioanal. Nucl. Chem. 232 (1–2): 139–41, doi:10.1007/BF02383729 .
The 20 common amino acids By propertiesAliphaticAromaticPolar, unchargedPositive charge (pKa)Negative charge (pKa)General Other classifications biochemical families: prot · nucl · carb (glpr, alco, glys) · lipd (fata/i, phld, strd, gllp, eico) · amac/i · ncbs/i · ttpy/i K→acetyl-CoAtryptophan→alanine→ GG→pyruvate→citrateG→glutamate→
α-ketoglutarateotherG→fumarateG→oxaloacetatesee urea cycle
Other Neurotransmitters Amino acids Endocannabinoids Gasotransmitters Monoamines Purines Trace amines OthersSee also Template:Neuropeptides Glycinergics Receptor
inhibitorsPlasmalemmalGlyT1 inhibitorsGlyT2 inhibitorsVIAAT Inhibitors
inhibitorsSHMT InhibitorsGDC InhibitorsDAAO Inhibitors
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