L-Alanine which is known also as Alanine is an amino acid. It is a non-polar amino acid and as abbreviated as Ala or A. L-Alanine is an α-amino acid with the chemical formula CH3CH (NH2) COOH.
The L-isomer is one of the 22 proteinogenic amino acids which are the building blocks of proteins.
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. Dietary sources 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.
L-Alanine is found in a wide variety of foods, but is particularly concentrated in meats.
Good sources of alanine include meat, seafood, caseinate, dairy products, eggs, fish, gelatin and lactalbumin.
Vegetarian sources of alanine is beans, nuts, seeds, soy, whey, brewer's yeast, brown rice, bran, corn, legumes, whole grains.
Biosynthesis Alanine can be manufactured in the body from pyruvate and branched chain amino acids such as valine, leucine, and isoleucine.
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.
Chemical synthesis 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: Physiological function Glucose–alanine cycle
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 An international study led by Imperial College London found a correlation between high levels of alanine and higher blood pressure, energy intake, cholesterol levels, and body mass index. (S)-Alanine and (R)-alanine in zwitterionic form at neutral pH