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L-Alanine is an α-amino acid that is used in the biosynthesis of proteins.
L-Alanine contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain.
Consequently, L-Alanines IUPAC systematic name is 2-aminopropanoic acid, and L-Alanine is classified as a nonpolar, aliphatic α-amino acid.
CAS Number: 56-41-7
EC Number: 200-273-8
IUPAC Name: 2-aminopropanoic acid
Chemical Formula: C3H7NO2
Other names: (2S)-2-Aminopropanoate, (2S)-2-Aminopropanoic acid, (S)-(+)-Alanine, (S)-2-amino-Propanoate, (S)-2-amino-Propanoic acid, (S)-2-Aminopropanoate, (S)-2-Aminopropanoic acid=(S)-Alanine, 2-Aminopropanoate, 2-Aminopropanoic acid, 2-Aminopropionate, 2-Aminopropionic acid, 2-Ammoniopropanoate, 2-Ammoniopropanoic acid, a-Alanine, a-Aminopropionate, a-Aminopropionic acid, Ala, Alanine, alpha-Alanine, alpha-Aminopropanoate, alpha-Aminopropanoic acid, alpha-Aminopropionate, alpha-Aminopropionic acid, L-(+)-Alanine, L-2-Aminopropanoate, L-2-Aminopropanoic acid, L-2-Aminopropionate, L-2 Aminopropionic acid, L-a-Alanine, L-a-Aminopropionate, L-a-Aminopropionic acid, L-alpha-Alanine, L-alpha-Aminopropionate, L-alpha-Aminopropionic acid, L-Alanin, L-Α-alanine, Abufène, Alanine doms-adrian brand, Alanine, L-isomer, Doms-adrian brand OF alanine, Doms adrian brand OF alanine, L-Isomer alanine, Alanine, L isomer, L Alanine, L-Alanin, L-Α-alanine, Abufène, Alanine doms-adrian brand, Alanine, L-isomer, Doms-adrian brand OF alanine, Doms adrian brand OF alanine, L Isomer alanine, Alanine, L isomer, L Alanine
Under biological conditions, L-Alanine exists in L-Alanines zwitterionic form with L-Alanines amine group protonated (as −NH3+) and L-Alanines carboxyl group deprotonated (as −CO2−).
L-Alanine is non-essential to humans as L-Alanine can be synthesised metabolically and does not need to be present in the diet.
L-Alanine is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG).
A nonessential amino acid in human. L-Alanine plays a key role in the glucose-L-Alanine cycle between muscle tissue and the liver.
L-Alanine is widely used as an ingredient in infusion and infant formula.
L-Alanine is an amino acid that is used to make proteins.
L-Alanine is used to break down tryptophan and vitamin B-6.
L-Alanine is a source of energy for muscles and the central nervous system.
L-Alanine strengthens the immune system and helps the body use sugars.
L-Alanine, a non-essential amino acid, is produced enzymatically from L-aspartate using aspartate β-decarboxylase.
Aminopropanoic acid is the smallest among all the aminoacids.
L-Alanine, USP/EP/JP, also known as 2-Aminopropanoic Acid, is a multi-compendial amino acid for your manufacturing needs.
L-Alanine, either of two amino acids, one of which, L-Alanine, or alpha-L-Alanine (α-L-Alanine), is a constituent of proteins.
An especially rich source of L-Alanine is silk fibroin, from which the amino acid was first isolated in 1879.
L-Alanine is one of several so-called nonessential amino acids for birds and mammals; i.e., they can synthesize Aminopropanoic acid from pyruvic acid (formed in the breakdown of carbohydrates) and do not require dietary sources.
L-Alanine (abbreviated as Ala or A) is an alpha-amino acid. The L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins.
Aminopropanoic acid is often classified as a nonpolar amino acid.
L-Alanine can be biosynthesized from pyruvate and branched chain amino acids such as valine, leucine, and isoleucine.
Aminopropanoic acid is most commonly produced by reductive amination of pyruvate.
L-Alanine is tightly coupled to metabolic pathways such as glycolysis, gluconeogenesis, and the citric acid cycle.
L-Alanine also arises together with lactate and generates glucose from protein degradation via the L-Alanine cycle.
L-Alanine's catabolic pathway involves a simple aminotransferase reaction that directly produces pyruvate.
Generally pyruvate produced by this pathway will result in the formation of oxaloacetate, although when the energy charge of a cell is low the pyruvate will be oxidized to CO2 and H2O via the pyruvate dehydrogenase complex and the citric acid cycle.
This makes L-Alanine a glucogenic amino acid.
L-Alanine is an amino acid commonly found as a component of total parenteral nutrition.
L-Alanine is the L-enantiomer of L-Alanine. Aminopropanoic acid has a role as an EC 4.3.1.15 (diaminopropionate ammonia-lyase) inhibitor and a fundamental metabolite.
L-Alanine is a pyruvate family amino acid, a proteinogenic amino acid, a L-alpha-amino acid and an L-Alanine.
L-Alanine is a conjugate base of a L-alaninium. Aminopropanoic acid is a conjugate acid of a L-alaninate.
L-Alanine is an enantiomer of a D-L-Alanine.
L-Alanine is a tautomer of a L-Alanine zwitterion.
D-L-Alanine, or beta-L-Alanine (β-L-Alanine), is not found in proteins but occurs naturally in two peptides, carnosine and anserine, found in mammalian muscle.
Aminopropanoic acid is an important constituent of the vitamin pantothenic acid.
L-Alanine is a Food for Special Medical Purposes for use under medical supervision.
A powdered form of the amino acid L-Alanine.
For use as a supplement in the dietary management of conditions requiring additional L-Alanine.
Suitable for use from birth.
Belongs to the class of organic compounds known as L-Alanine and derivatives.
L-Alanine and derivatives are compounds containing L-Alanine or a derivative thereof resulting from reaction of L-Alanine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
L-Alanine is a non-essential amino acid that occurs in high levels in its free state in plasma.
L-Alanine is produced from pyruvate by transamination.
L-Alanine is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system.
L-Alanine (Ala), also known as L-Alanine 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.
L-Alanine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins.
L-Alanine is found in all organisms ranging from bacteria to plants to animals.
L-alpha-Aminopropionic acid is classified as an aliphatic, non-polar amino acid.
In humans, L-Alanine is a non-essential amino acid that can be easily made in the body from either the conversion of pyruvate or the breakdown of the dipeptides carnosine and anserine.
L-Alanine can be also synthesized from branched chain amino acids such as valine, leucine, and isoleucine.
L-Alanine is produced by reductive amination of pyruvate through a two-step process.
In the first step, alpha-ketoglutarate, ammonia and NADH are converted by the enzyme known glutamate dehydrogenase to glutamate, NAD+ and water.
In the second step, the amino group of the newly-formed glutamate is transferred to pyruvate by an aminotransferase enzyme, regenerating the alpha-ketoglutarate, and converting the pyruvate to L-Alanine.
The net result is that pyruvate and ammonia are converted to L-Alanine.
In mammals, L-Alanine plays a key role in glucose-L-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 to pyruvate, a L-Alanine of muscle glycolysis, through the action of L-Alanine aminotransferase, forming L-Alanine and alpha-ketoglutarate.
The L-Alanine enters the bloodstream and is transported to the liver.
The L-Alanine aminotransferase reaction takes place in reverse in the liver, where the regenerated pyruvate is used in gluconeogenesis, forming glucose which returns to the muscles through the circulation system.
L-Alanine is highly concentrated in muscle and is one of the most important amino acids released by muscle, functioning as a major energy source.
Plasma L-Alanine is often decreased when the BCAA (branched-chain amino acids) are deficient.
This finding may relate to muscle metabolism. L-Alanine is highly concentrated in meat L-Alanines and other high-protein foods like wheat germ and cottage cheese.
L-Alanine is an important participant as well as a regulator of glucose metabolism.
L-Alanine levels parallel blood sugar levels in both diabetes and hypoglycemia, and L-Alanine is reduced in both severe hypoglycemia and the ketosis of diabetes.
L-Alanine is an important amino acid for lymphocyte reproduction and immunity.
L-Alanine therapy has helped dissolve kidney stones in experimental animals.
Normal L-Alanine metabolism, like that of other amino acids, is highly dependent upon enzymes that contain vitamin B6.
L-Alanine, like GABA, taurine, and glycine, is an inhibitory neurotransmitter in the brain.
L-Alanine1 and L-serine1 are amino acids that are necessary for the biosynthesis of proteins.
They are considered “nonessential” in human diets (and those of most other animals) because they are synthesized in the body.
In 1850, long before it was discovered in and isolated from natural substances, L-Alanine was synthesized from acetaldehyde by German chemist Adolph Strecker.
Of course, Strecker made the D,L-racemate of the amino acid rather than either isomer alone.
Serine, on the other hand, was first discovered in nature, specifically in silk protein, by German chemist Emil Cramer in 1865. And, speaking of silk . . .
L-Alanine and serine, along with previous Molecules of the Week glycine and L-proline, are the major amino acids in spider silk proteins.
L-Alanine-rich crystalline areas give silk strength, whereas glycine-rich amorphous regions provide elasticity
L-Alanine is a non-essential amino acid with the abbreviation of A or Ala.
L-Alanine is one of the twenty amino acids needed for life function, but it is defined as non-essential.
Make sure not to get non-essential confused with 'not needed,' however.
All non-essential means in terms of amino acids is that the body can produce it rather than needing to obtain it through outside food sources.
L-Alanine is a non-essential amino acid that occurs in high levels in its free state in plasma.
L-Alanine is is produced from pyruvate by transamination.
L-Alanine is is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system
Application
L-Alanine has been used as a supplement in complete medium for cell culture.
The L-isomer of L-Alanine (left-handed) is the one that is incorporated into 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.
The right-handed form, D-L-Alanine, occurs in polypeptides in some bacterial cell walls: 131 and in some peptide antibiotics, and occurs in the tissues of many crustaceans and molluscs as an osmolyte.
L-Alanine is also very abundant (over-represented) in low complexity regions of proteins.
L-Alanine for biochemistry.
CAS 56-41-7, pH 5.5 - 6.5 (100 g/l, H₂O, 20 °C).
Alpha-L-Alanine is used for low blood sugar (hypoglycemia), diarrhea-related dehydration, liver disease, enlarged prostate (benign prostatic hypertrophy, BPH), fatigue, stress, and certain inherited disorders including glycogen storage disease and urea cycle disorders.
Amino acids are available as single amino acids or in amino-acid combinations.
They’re in multivitamin formulas, proteins, and food supplements.
The forms they come in include tablets, fluids, and powders.
If you eat enough protein in your diet, you should be getting all the amino acids you need.
The Structure of L-Alanine
In general, all amino acids have the same structure: an amino group attached to a hydrogen, a carboxyl group, and a side chain group that's denoted by 'R' via a central carbon.
The amino and carboxyl groups and central carbon are considered the amino acid backbone.
This backbone is the same in all amino acids.
L-alpha-Aminopropionic acid's the side chain that is specific to each individual type of amino acid.
The specific structure of L-Alanine is indicative of its chemical formula, CH3.
This is simply the backbone of the amino acid structure with a methyl group attached as a side chain.
Methyl groups are cleaved regularly in normal body functions, making this amino acid simple to synthesize.
L-Alanine is a non-polar amino acid.
L-alpha-Aminopropionic acid has a linear confirmation and is non-reactive.
Because of this non-reactivity, the amino acid is not important in protein function, despite its large prevalence in amino acids within the body.
This amino acid is typically 7.8% of the primary structure of proteins.
Alpha-L-Alanine is a non-essential amino acid.
Non-essential amino acids can be made by the body, so they don’t have to be provided by food.
Amino acids are the building blocks of proteins.
You may see the terms “L-alpha-L-Alanine” and “D-alpha-L-Alanine.“
The “L” refers to the “left-handed” chemical form of the alpha-L-Alanine molecule.
The “D” refers to the “right-handed” chemical form of the molecule.
The L and D forms are mirror-images of each other.
Alpha-L-Alanine is used for low blood sugar (hypoglycemia), diarrhea-related dehydration, liver disease, enlarged prostate (benign prostatic hypertrophy, BPH), fatigue, stress, and certain inherited disorders including glycogen storage disease and urea cycle disorders.
Biosynthesis
L-Alanine can be synthesized from pyruvate and branched chain amino acids such as valine, leucine, and isoleucine.
L-Alanine is produced by reductive amination of pyruvate, a two-step process.
In the first step, α-ketoglutarate, ammonia and NADH are converted by glutamate dehydrogenase to glutamate, NAD+ and water.
In the second step, the amino group of the newly-formed glutamate is transferred to pyruvate by an aminotransferase enzyme, regenerating the α-ketoglutarate, and converting the pyruvate to L-Alanine.
The net result is that pyruvate and ammonia are converted to L-Alanine, consuming one reducing equivalent. Because transamination reactions are readily reversible and pyruvate is present in all cells, L-Alanine can be easily formed and thus has close links to metabolic pathways such as glycolysis, gluconeogenesis, and the citric acid cycle.
Chemical synthesis
L-Alanine is produced industrially by decarboxylation of L-aspartate by the action of aspartate 4-decarboxylase.
Fermentation routes to L-Alanine are complicated by L-Alanine racemase.[14]
Racemic L-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.
Degradation
L-Alanine is broken down by oxidative deamination, the inverse reaction of the reductive amination reaction described above, catalyzed by the same enzymes.
The direction of the process is largely controlled by the relative concentration of the substrates and L-Alanines of the reactions involved.
Substituents
L-Alanine or derivatives
Alpha-amino acid
L-alpha-amino acid
Amino acid
Carboxylic acid
Monocarboxylic acid or derivatives
Hydrocarbon derivative
Organic oxygen compound
Primary amine
Organooxygen compound
Organonitrogen compound
Organic nitrogen compound
Primary aliphatic amine
Carbonyl group
Amine
Organopnictogen compound
Organic oxide
Aliphatic acyclic compound
Key features and details
Assay type: Quantitative
Detection method: Colorimetric/Fluorometric
Platform: Microplate reader
Assay time: 40 min
Sample type: Cell culture supernatant, Other biological fluids, Plasma, Serum, Tissue Extracts, Urine
Sensitivity: 24 µg/ml
L-Alanine World Hypothesis
L-Alanine is one of the twenty canonical α-amino acids used as building blocks (monomers) for the ribosome-mediated biosynthesis of proteins.
L-Alanine is believed to be one of the earliest amino acids to be included in the genetic code standard repertoire.
On the basis of this fact the "L-Alanine World" hypothesis was proposed.
This hypothesis explains the evolutionary choice of amino acids in the repertoire of the genetic code from a chemical point of view.
In this model the selection of monomers (i.e. amino acids) for ribosomal protein synthesis is rather limited to those L-Alanine derivatives that are suitable for building α-helix or β-sheet secondary structural elements.
Dominant secondary structures in life as we know 2-amino-Propanoic acid are α-helices and β-sheets and most canonical amino acids can be regarded as chemical derivatives of L-Alanine.
Therefore, most canonical amino acids in proteins can be exchanged with Ala by point mutations while the secondary structure remains intact.
The fact that Ala mimics the secondary structure preferences of the majority of the encoded amino acids is practically exploited in L-Alanine scanning mutagenesis.
In addition, classical X-ray crystallography often employs the polyL-Alanine-backbone model to determine three-dimensional structures of proteins using molecular replacement - a model-based phasing method.
