3775-73-3

Basic information

• Product Name: (R)-3-AMINOBUTYRIC ACID
• Synonyms: (R)-B-AMINOBUTYRIC ACID;RARECHEM LK HD C012;(R)-3-AMINOBUTYRIC ACID;(R)-3-aminobutanoic acid;D-3-Abu-OH;L-3-Abu-OH;(R)-beta-homo-alanine;(R)-HOMO-BETA-ALANINE
• CAS NO: 3775-73-3
• Molecular Formula: C₄H₉NO₂
• Molecular Weight: 103.12
• Mol File: 3775-73-3.mol

Chemical Properties

• Melting Point: 215-216 °C
• Boiling Point: 223.6 °C at 760 mmHg
• Flash Point: 89 °C
• Appearance: /
• Density: 1.105 g/cm³
• Storage Temp.: Keep in dark place,Sealed in dry,Room Temperature
• Solubility: Methanol (Slightly), Water (Slightly, Sonicated)
• PKA: 3.67±0.12(Predicted)
• CAS DataBase Reference: (R)-3-AMINOBUTYRIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-3-AMINOBUTYRIC ACID(3775-73-3)
• EPA Substance Registry System: (R)-3-AMINOBUTYRIC ACID(3775-73-3)

Safety Data

• Hazardous Substances Data: 3775-73-3(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
(R)-3-Aminobutyric Acid is used as a key intermediate in the synthesis of fused ring Pyrimidone derivatives, which are crucial for the treatment of Hepatitis B Virus (HBV) infection and HBV-induced diseases. Its role in the development of these therapeutic agents highlights its importance in the pharmaceutical sector.
Used in Chemical Synthesis:
As a versatile building block, (R)-3-Aminobutyric Acid is utilized in various chemical synthesis processes, particularly in the creation of complex organic molecules and pharmaceutical compounds. Its unique structure and reactivity make it a valuable asset in the development of novel drugs and materials.

Upstream product

• 21948-18-5 (S)-3-amino-4-methylsulfanyl-butyric acid 
• 67843-72-5 (R)-3-(((benzyloxy)carbonyl)amino)butanoic acid 
• 134430-94-7 benzyl (3R,αR)-3-(N-benzyl-N-α-methylbenzylamino)butanoate 
• 132540-67-1 (R)-3-(dibenzylamino)butanoic acid 
• 141632-86-2 (1'S,6R)-1-benzyloxycarbonyl-3-(1'-phenyleth-1'-yl)-6-methylperihydropyrimidin-4-one 
• 64838-60-4 (3R,1'S)-3-<(1'-phenylethyl)amino>butanoic acid methyl ester 
• 147228-34-0 (3R)-3-(tosylamino)butanoic acid 
• 623-43-8 crotonic acid methyl ester 
• 394220-59-8 N-p-methoxybenzyl-3-methylisoxazolidin-5-one 
• 120686-16-0 tert-butyl (R)-3-amino-3-methyl-propionate 
• 1067647-39-5 (R)-3-butanamidobutanoic acid tert-butyl ester 
• 107-93-7 (E)-but-2-enoic acid 
• 95503-53-0 3-[Hydroxy-((S)-1-phenyl-ethyl)-amino]-butyric acid methyl ester 

Downstream Products

• 86-14-6 (R)-diethyl-(1-methyl-3,3-di-[2]thienyl-allyl)-amine 
• 139243-54-2 (R)-3-aminobutanoic acid methyl ester hydrochloride 
• 158462-50-1 R(+)-3-(trifluoroacetamido)butanoic acid 
• 113034-29-0 (R)-3-(benzoylamino)butanoic acid 
• 67843-72-5 (R)-3-(((benzyloxy)carbonyl)amino)butanoic acid 
• 120686-16-0 tert-butyl (R)-3-amino-3-methyl-propionate 
• 1392843-06-9 (R)-3-[(1-Benzyl-5-hydroxy-2-oxo-3-phenyl-1,2-dihydro-[1,7]naphthyridine-6-carbonyl)-amino]-butyric acid 
• 159991-23-8 (R)-3-((tert-butoxycarbonyl)amino)butanoic acid 
• 1455088-28-4 3-(R)-[(1-cyano-4-hydroxy-7-phenoxyisoquinoline-3-carbonyl)amino]butyric acid 
• 1460306-61-9 C₇H₁₃NO₂*ClH 
• 1620680-34-3 (R)-3-formamidobutanoic acid 
• 6078-06-4 (R)-methyl 3-aminobutanoate hydrochloride 

Relevant articles and documents

Michael-type addition of phthalimide salts to chiral α,β-unsaturated imides

The synthesis of (R)-(-)-3-aminobutanoic acid starting from chiral α,β- unsaturated imide 1b is described, by means of the nucleophilic attack of several phthalimido derivatives in the presence of a Lewis acid. The reaction was studied in some details and chloromagnesium phthalimide afforded the better results with 95:5 diastereomeric ratio and 90% yield. Furthermore the resulting enolate was trapped performing the reaction in the presence of benzenesulfonyl bromide and the 2-bromo-3-phthalimido derivative 4 was obtained in good yield and high diastereoselectivity and successively transformed into the corresponding 2-azido-3-phthalimido derivative 6 by displacement of the bromide with sodium azide.

Converting aspartase into a β-amino acid lyase by cluster screening

Aspartase, despite being one of the most specific enzymes known, shows potential for application in β-amino acid synthesis. The substrate binding pocket of AspB from Bacillus sp. YM55-1 was reshaped by enzyme engineering to accommodate crotonic acid. The mutant enzyme BSASP-C6 yielded enantiopure (R)-3-aminobutyrate from crotonic acid and ammonia. To obtain this mutant, a high-throughput screening in combination with a focused permutational library was decisive for the success in this project. We achieved this by simultaneous randomisation of four residues within the substrate binding pocket and cluster screening in mixed population. Screening of 300 000 clones was necessary to find the BSASP-C6 mutant which has β-amino acid lyase activity. This exemplifies the need for efficient search and screening strategies in creating novel enzyme activities. The BSAPS-C6 enzyme developed here surpasses the natural substrate functionality of aspartase and thus represents the proof-of-concept of application of this novel synthetic route to a broader set of β-amino acids. β-Amino acids with aspartase mutants: Aspartase, despite being one of the most specific enzymes known, shows potential for application in β-amino acid synthesis. By applying a combination of focused library design and cluster screening, we created an aspartate mutant with β-amino acid lyase activity and thus open up a new platform to synthesize this interesting and important compound class. BSASP-C6= Mutant of AspB from Bacillus sp. YM55-1.

Preparation method of 3-aminopropanol or 3-aminopropionic acid derivative

The invention provides a preparation method of an optically active 3-aminopropanol or 3-aminopropionic acid derivative, and belongs to the technical field of organic synthesis. A compound having a structure as shown in a formula II and a formula III is used as a raw material, and the optically active 3-aminopropanol or 3-aminopropionic acid derivative is obtained through four basic steps, namely dehydration condensation, hydrogenation reduction, reduction and hydrolysis. The raw materials adopted in the preparation method are easy to obtain and low in cost; as a chiral phosphine-transitional metal catalyst is used in the hydrogenation reduction reaction, the optically active 3-aminopropanol or 3-aminopropionic acid derivative is efficient, high in selectivity, low in cost and suitable forlarge-scale production. Compared with existing chemical resolution and chiral introduction, the asymmetric hydrogenation synthesis method provided by the invention only produces one chiral product, ishigh in yield, and has relatively high advantages in economy and raw material utilization rate.

A optically active 3 - amino butanol and 3 - aminobutyric acid preparation method (by machine translation)

The invention discloses a method of optically active 3 - amino butanol and 3 - aminobutyric acid preparation method. Wherein optically active 3 - amino butyl alcohol preparation method comprises the following steps: in a solvent, in the borohydride reducing agent and a Lewis acid under the action of the, shown as 65 shown in the reduction reaction of compound, production like type 14 indicated by the compound. Optically active 3 - aminobutyric acid preparation method comprises the following steps: shown as 64 a compound represented by the hydrolytic reaction, production like type 65 compound of formula. Preparation method of this invention the raw material is cheap, simple operation, the process route is short, the raw material is not hazardous, high yield, produce little material waste, is beneficial for the protection of the environment, high conversion rate of raw materials, product chemical purity and high optical purity, and is easy to realize industrial. (by machine translation)

Cyclombandakamines A1 and A2, Oxygen-Bridged Naphthylisoquinoline Dimers from a Congolese Ancistrocladus Liana

Cyclombandakamines A1 (1) and A2 (2), both with an unprecedented pyrane-cyclohexenone-dihydrofuran sequence and six stereocenters and two chiral axes, are the first oxygen-bridged dimeric naphthylisoquinoline alkaloids. They were isolated from the leaves of an as yet unidentified Congolese Ancistrocladus species. Their stereostructures were established by spectroscopic, chemical, and chiroptical methods in combination with DFT and TDDFT calculations. They apparently originate from a cascade of oxidative cyclization reactions of open-chain naphthylisoquinoline dimers and exhibit significant antiprotozoal activities.

Acylation of β-Amino Esters and Hydrolysis of β-Amido Esters: Candida antarctica Lipase A as a Chemoselective Deprotection Catalyst

N-Acylation by lipase A from Candida antarctica (CAL-A) in ethyl butanoate was applied to the kinetic resolution of tert-butyl esters of 3-amino-3-phenylpropanoic acid (E>100), 3-amino-4-methylpentanoic acid (E>100) and 3-aminobutanoic acid (E=60) on 1.0-2.0 m scale. With the N-acylated resolution products, the exceptional ability of CAL-A to hydrolyse amides and bulky tert-butyl esters was then studied. In all N-acylated tert-butyl esters, chemoselectivity favoured the amide bond cleavage. The tert-butyl ester bond was left intact with 3-amino-3-phenylpropanoate, whereas with 3-amino-4-methylpentanoate and 3-aminobutanoate the CAL-A-catalysed hydrolysis of tert-butyl ester followed the amide hydrolysis.

METHOD FOR OBTAINING OPTICALLY PURE AMINO ACIDS

This invention relates to a method for obtaining optically pure amino acids, including optical resolution and optical conversion. This method significantly shortens the time taken for optical transformation, and enables the repeated use of an organic solution containing a enantioselective receptor, to thereby obtain optically pure amino acids in a simple and remarkably efficient manner, and to enable the very economical mass production of optically pure amino acids.

METHOD FOR OBTAINING OPTICALLY PURE AMINO ACIDS

This invention relates to a method for obtaining optically pure amino acids, including optical resolution and optical conversion. This method significantly shortens the time taken for optical transformation, and enables the repeated use of an organic solution containing a enantioselective receptor, to thereby obtain optically pure amino acids in a simple and remarkably efficient manner, and to enable the very economical mass production of optically pure amino acids.

Formation and hydrolysis of amide bonds by lipase A from Candida antarctica; Exceptional features

Various commercial lyophilized and immobilized preparations of lipase A from Candida antarctica (CAL-A) were studied for their ability to catalyze the hydrolysis of amide bonds in N-acylated α-amino acids, 3-butanamidobutanoic acid (β-amino acid) and its ethyl ester. The activity toward amide bonds is highly untypical of lipases, despite the close mechanistic analogy to amidases which normally catalyze the corresponding reactions. Most CAL-A preparations cleaved amide bonds of various substrates with high enantioselectivity, although high variations in substrate selectivity and catalytic rates were detected. The possible role of contaminant protein species on the hydrolytic activity toward these bonds was studied by fractionation and analysis of the commercial lyophilized preparation of CAL-A (Cat#ICR-112, Codexis). In addition to minor impurities, two equally abundant proteins were detected, migrating on SDS-PAGE a few kDa apart around the calculated size of CAL-A. Based on peptide fragment analysis and sequence comparison both bands shared substantial sequence coverage with CAL-A. However, peptides at the C-terminal end constituting a motile domain described as an active-site flap were not identified in the smaller fragment. Separated gel filtration fractions of the two forms of CAL-A both catalyzed the amide bond hydrolysis of ethyl 3-butanamidobutanoate as well as the N-acylation of methyl pipecolinate. Hydrolytic activity towards N-acetylmethionine was, however, solely confined to the fractions containing the truncated form of CAL-A. These fractions were also found to contain a trace enzyme impurity identified in sequence analysis as a serine carboxypeptidase. The possible role of catalytic impurities versus the function of CAL-A in amide bond hydrolysis is further discussed in the paper. The Royal Society of Chemistry 2010.

Burkholderia cepacia lipase and activated β-lactams in β-dipeptide and β-amino amide synthesis

The work describes fluorine-activated and N-Boc-activated β-lactams as acyl donors to N-nucleophiles in the presence of Burkholderia cepacia lipase (lipase PS-D). Fluorine activation at the β-lactam ring causes the ring to open in high enantioselectivity