beta-Alanine

Base Information

• Chemical Name: beta-Alanine
• CAS No.: 107-95-9
• Deprecated CAS: 87867-95-6
• Molecular Formula: C3H7NO2
• Molecular Weight: 89.0941
• Hs Code.: 29224920
• European Community (EC) Number: 203-536-5
• NSC Number: 7603
• UNII: 11P2JDE17B
• DSSTox Substance ID: DTXSID0030823
• Nikkaji Number: J4.070C
• Wikipedia: %CE%92-Alanine
• Wikidata: Q310919
• RXCUI: 61
• Pharos Ligand ID: B9FVNSQTPFN2
• Metabolomics Workbench ID: 37049
• ChEMBL ID: CHEMBL297569
• Mol file: 107-95-9.mol

Synonyms:3 Aminopropionic Acid;3-Aminopropionic Acid;beta Alanine;beta Alanine Hydrochloride;beta Alanine, Monopotassium Salt;beta Alanine, Monosodium Salt;beta-Alanine;beta-Alanine Hydrochloride;beta-Alanine, Calcium Salt (2:1);beta-Alanine, Monopotassium Salt;beta-Alanine, Monosodium Salt;Hydrochloride, beta-Alanine

Chemical Property of beta-Alanine

Chemical Property:

• Appearance/Colour: white crystalline powder
• Melting Point: 202 °C (dec.)(lit.)
• Refractive Index: 1.4650 (estimate)
• Boiling Point: 237.1 °C at 760 mmHg
• PKA: 3.55(at 25℃)
• Flash Point: 97.2 °C
• PSA: 63.32000
• Density: 1.166 g/cm³
• LogP: 0.12010
• Storage Temp.: Store at RT.
• Solubility.: H2O: 1 M at 20 °C, clear, colorless
• Water Solubility.: Soluble in water(550g/L). Slightly soluble in alcohol. Insoluble in ether and acetone.
• XLogP3: -3
• Hydrogen Bond Donor Count: 2
• Hydrogen Bond Acceptor Count: 3
• Rotatable Bond Count: 2
• Exact Mass: 89.047678466
• Heavy Atom Count: 6
• Complexity: 52.8

Purity/Quality:

98.0% ^*data from raw suppliers

b-Alanine ^*data from reagent suppliers

Safty Information:

• Pictogram(s): Xi
• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 24/25-36-26

MSDS Files:

SDS file from LookChem

Useful:

• Chemical Classes: Other Uses -> Biochemical Research
• Canonical SMILES: C(CN)C(=O)O
• Recent ClinicalTrials: Beta-alanine Supplementation and CrossFit Performance
• Description: Beta-alanine is a non-proteogenic amino acid that is produced endogenously in the liver. In addition, humans acquire beta-alanine through the consumption of foods such as poultry and meat. By itself, the ergogenic properties of beta-alanine are limited; however, beta-alanine has been identified as the rate-limiting precursor to carnosine synthesis, and has been consistently shown to increase levels of carnosine in human skeletal muscle. Doses of 4 to 6 g/day of beta-alanine have been shown to increase muscle carnosine concentrations by up to 64 % after 4 weeks, and up to 80 % after 10 weeks. Baguet et al. demonstrated that individuals vary in the magnitude of response to 5 to 6 weeks of betaalanine supplementation (4.8 g/day), with high responders increasing muscle carnosine concentrations by an average of 55 %, and low responders increasing by an average of only 15 %. The difference between high and low responders seems, at least in part, to be related to baseline muscle carnosine content and muscle fiber composition. β-Alanine, a β?amino acid, is a component of pantothenic acid and the rate-limiting amino acid in the biosynthesis of the histidinyl antioxidant dipeptides carnosine and anserine. Endogenous β-amino acid that is a nonselective agonist at glycine receptors and a ligand for the G protein-coupled orphan receptor, TGR7 (MrgD). β-Alanine flux plays a cytoprotective role by supporting the osmotic stability of marine organisms, preimplantation mouse embryos and mammalian cells exposed to hypoxic stress. β-Alanine (or beta-alanine) is a naturally occurring beta amino acid, which is an amino acid in which the amino group is at the β- position from the carboxylate group (i.e., two atoms away. The IUPAC name for β-alanine is 3-amino propanoic acid. Unlike its counterpart α-alanine, β-alanine has no stereocenter. β-Alanine is not used in the biosynthesis of any major proteins or enzymes. It is formed in vivo by the degradation of dihydrouracil and carnosine. It is a component of the naturally occurring peptides carnosine and anserine and also of pantothenic acid (vitamin B5), which itself is a component of coenzyme A. Under normal conditions, β-alanine is metabolized into acetic acid. β-Alanine is the rate-limiting precursor of carnosine, which is to say carnosine levels are limited by the amount of available β-alanine. Supplementation with β-alanine has been shown to increase the concentration of carnosine in muscles, decrease fatigue in athletes and increase total muscular work done.Typically, studies have used supplementing strategies of multiple doses of 400 mg or 800 mg, administered at regular intervals for up to eight hours, over periods ranging from 4 to 10 weeks . After a 10 - week supplementing strategy, the reported increase in intramuscular carnosine content was an average of 80.1% (range 18 to 205%).
• Uses: It is widely used in medicine, feed, food, and other industries, mostly to synthesize pantothenic acid and calcium pantothenate (a medicine and feed additive), carnosine, pamidronate sodium, barley nitrogen. It is also used to produce plating corrosion inhibiter, as a biological reagent, and as an organic synthesis intermediate. Used as a food and health supplement additive. Endogenous beta-amino acids, non-selective glycine receptor agonists ，G-protein-coupled orphan receptor (TGR7, MrgD) ligand. Relying on the stability of marine biology, beta-aminopropionic acid has a protective effect on cells. Effective catalyst for the Knoevenagel condensation. Beta Alanine is used as nutrition supplements in food production. Increase muscular strength & power output, Increases Muscle Mass, increase Anaerobic Endurance. β-Alanine is a naturally occurring beta amino acid. β-Alanine is formed in vivo by the degradation of dihydrouracil (D449990) and carnosine. β-Alanine is also the rate-limiting precursor of carnosine, as a result supplementation with β-alanine increases the concentration of carnosine in muscles. β-Alanine has been used as a ligand for the orphan MAS-related receptor. It has also been used in culture media used for certain strains of yeast to test for β-alanine auxotrophy.
• Biological Functions: β-alanine is a non-essential amino acid that can potentially indirectly enhance performance of extremely high intensity (110% of VO2 peak), short duration (1-5 minutes) bouts of exercise. β-alanine may enhance performance by increasing intramuscular levels of another amino acid, carnosine. It is well established that acidosis can increase fatigue during exercise and therefore increasing the body’s buffering capacity may improve high-intensity, short-duration exercise performance. The importance of carnosine has been previously described by Tallon et al., who reported carnosine concentrations in body builders of 40 mmol/kg dry mass compared to the average human of 16 mmol/kg dry mass. Tallon et al. estimated carnosine to account for 20% of total buffering capacity in body builders compared to 10% in the typical population. In theory, if an athlete of any age increases the amount of carnosine present in skeletal muscle, they can enhance their ability to buffer acidic concentrations during high-intensity exercise and thus delay fatigue.

Technology Process of beta-Alanine

There total 220 articles about beta-Alanine which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:

Reference yield:

β-Ala-OPNP (87880-78-2) → 4-nitro-phenol (100-02-7,78813-13-5,89830-32-0) + 3-amino propanoic acid (107-95-9)

Guidance literature:

With Cu complex of polymer from 2,6-bis-aminomethylpyridine and 4,4'-bis-aminomethyldiphenylmethane; water; In dimethyl sulfoxide; at 25 ℃; Rate constant; var.reag.: Cu⁽²⁺⁾ complex of 2,6-bis-benzylaminomethylpyridine; oligomers of 2,6-bis-aminomethylpyridine and 4,4'-bis-aminomethyldiphenylmethane;

DOI:10.1002/(sici)1099-0690(199806)1998:6<1143::aid-ejoc1143>3.0.co;2-u

Reference yield:

deoxythymidylyl-(5'->N)-β-alanine (85590-80-3) → thymidine 5'-phosphate (365-07-1,15108-71-1,60363-32-8,96744-88-6,132696-16-3,143838-77-1) + 3-amino propanoic acid (107-95-9)

Guidance literature:

With hydrogenchloride; water; at 37 ℃; for 1h; Product distribution; hydrolytic stability at various pH;

DOI:10.1007/BF00579428

Reference yield:

leucinostatin A (82111-44-2) → (2S,3S)-3-hydroxyleucine (10148-70-6) + cis-4-methyl-(S)-proline (6734-41-4) + 2-Aminoisobutyric acid (62-57-7) + 3-amino propanoic acid (107-95-9)

Guidance literature:

With hydrogenchloride; at 110 ℃; for 20h; Further byproducts given;

DOI:10.1039/c39820000094

upstream raw materials:

piperidine

3-Bromopropionic acid

Succinimide

3-phthalimidopropionitrile

Downstream raw materials:

methyl 3-aminopropanoate

2-<2-Carboxy-ethyl-imino>-hexahydro-azepin

3-succinimidopropionic acid

3-[N-(2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)amino]propionic acid

Refernces

Assymetric synthesis of (2S,3R)- and (2S,3S)-[2-¹³C;3-²H] glutamic acid

10.1016/j.tetlet.2009.01.062

The research aims to develop a synthetic route for these specific isotopically labeled glutamic acids with high enantioselectivity for metabolic analysis. The study employs key chemicals such as [2-13C] glycine, β-alanine, lithium aluminum deuteride (LiAlD4), and the (S,S)-Et-DuPHOS-Rh catalyst. The synthesis involves the preparation of a stable isotope-labeled dehydroornithine derivative through the Horner–Wadsworth–Emmons reaction, followed by asymmetric hydrogenation or deuteration using the (S,S)-Et-DuPHOS-Rh catalyst. Ruthenium-catalyzed oxidation is then used to convert the intermediate to the target glutamic acids. The enantiopurity of the final products is confirmed to be 99% ee by HPLC analysis. The research concludes that the asymmetric synthesis of (2S,3R)- and (2S,3S)-[2-13C;3-2H] glutamic acids has been successfully achieved with high enantioselectivity, and modifications to this procedure for synthesizing other labeled amino acids are underway.

An Efficient Chemoenzymatic Synthesis of Coenzyme A and Its Disulfide

10.1021/acs.oprd.6b00059

The study presents an efficient chemoenzymatic synthesis route for coenzyme A (CoASH) and its disulfide, which is scalable to gram quantities using standard laboratory equipment. The key innovation is the use of pantethine, a disulfide derivative of pantetheine, as the biocatalytic precursor. This approach eliminates the need for a sulfhydryl protecting group and prevents sulfur oxidation by-products. The synthesis involves a five-step process starting from ?-alanine, yielding pantethine with a 76% overall yield. The three enzymes of the CoASH salvage pathway—pantetheine kinase (PanK), phosphopantetheine adenyltransferase (PPAT), and dephospho-coenzyme A kinase (DPCK)—are used to convert pantethine into CoA disulfide, a more stable form of the cofactor. The final product, CoA disulfide, can be reduced in situ to free CoASH for biochemical applications. The method avoids chromatography until the final step, facilitating scale-up, and the disulfide form of CoASH is more stable and valuable than the free thiol form.

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