40469-85-0

Basic information

• Product Name: (S)-HOMO-BETA-VALINE
• Synonyms: (S)-HOMO-BETA-VALINE ;REF DUPL: (S)-beta-homovaline;L-β-Hoval-OH;Pentanoic acid, 3-amino-4-methyl-, (3S)-
• CAS NO: 40469-85-0
• Molecular Formula: C₆H₁₃NO₂
• Molecular Weight: 131.174
• Mol File: 40469-85-0.mol

Chemical Properties

• Melting Point: 202-210℃ (decomposition)
• Boiling Point: 232 °C at 760 mmHg
• Flash Point: 94.1 °C
• Appearance: /
• Density: 1.035 g/cm³
• Vapor Pressure: 0.0212mmHg at 25°C
• Refractive Index: 1.462
• Storage Temp.: Sealed in dry,Room Temperature
• PKA: 3.81±0.10(Predicted)
• CAS DataBase Reference: (S)-HOMO-BETA-VALINE(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-HOMO-BETA-VALINE(40469-85-0)
• EPA Substance Registry System: (S)-HOMO-BETA-VALINE(40469-85-0)

Safety Data

• Hazardous Substances Data: 40469-85-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
(S)-Homo-beta-valine is used as a building block for the synthesis of various pharmaceuticals due to its unique chemical properties, which allow for the creation of novel drug molecules with potential therapeutic applications.
Used in Biotechnology Industry:
In the biotechnology sector, (S)-Homo-beta-valine is utilized as a component in the development of new biological products, leveraging its distinctive biological properties to enhance or create innovative solutions.
Used in Peptide Synthesis:
(S)-Homo-beta-valine is used as a key component in peptide synthesis, contributing to the structural and functional diversity of peptides for research and therapeutic purposes.
Used in Antibiotic Production:
As an important constituent of certain antibiotics, (S)-Homo-beta-valine plays a crucial role in the development and effectiveness of these life-saving medications.
Used in Antiviral Agent Development:
(S)-Homo-beta-valine is also used in the formulation of antiviral agents, where its unique properties can contribute to the inhibition or treatment of viral infections.

InChI:InChI=1/C6H13NO2/c1-4(2)5(7)3-6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1

Upstream product

• 72342-64-4 methyl (3S)-3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-4-methylpentanoate 
• 58543-97-8 (3R)-3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-4-methylpentanoic acid 
• 61-90-5 L-leucine 
• 172695-23-7 (R)-3-<(tert-butoxycarbonyl)amino>-4-methylpentanenitrile 
• 13734-41-3 t-Boc-L-valine 
• 72-18-4 L-valine 
• 5115-65-1 (R)-N-phthaloylvaline 
• 72212-78-3 (R)-2-(1,3-dioxoisoindolin-2-yl)-3-methylbutanoyl chloride 
• 5699-54-7 3-amino-4-methylpentanoic acid 
• 122818-28-4 (S)-2-(N-tert-butoxycarbonylamino)-3-methylbutyl tosylate 
• 79069-14-0 (S)-2-<(tert-butoxycarbonyl)amino>-3-methylbutan-1-ol 

Downstream Products

• 61-90-5 L-leucine 
• 78175-31-2 (R)-3-(2,4-Dinitro-phenylamino)-4-methyl-pentanoic acid 
• 215608-32-5 (R)-3-<(benzyoxycarbonyl)amino>-4-methylpentanoic acid 
• 215608-34-7 methyl (R)-4-<(benzyloxycarbonyl)amino>-5-methyl-2-oxohexanoate 
• 215608-40-5 methyl (2R,4R)-4-<(benzyloxycarbonyl)amino>-2-hydroxy-5-methylhexanoate 
• 78175-26-5 (R)-3-(2,4-Dinitro-phenylamino)-4-methyl-pentanoic acid (4-methoxy-phenyl)-amide 
• 1381761-98-3 1-((R)-1-((((2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)(methyl)amino)-4-methylpentan-3-yl)-3-(4-(tert-butyl)phenyl)urea 
• 112121-72-9 Methyl (R)-(-)-N-benzyloxycarbonylamino-4-methylpentanoate 
• 791131-00-5 (R)-3-(benzyloxycarbonylamino)-4-methylpentanal 
• 1381761-95-0 benzyl((R)-1-((((3aR,4R,6R,6aR)-6-(6-amino-9H-purin-9-yl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methyl)(methyl)amino)-4-methylpentan-3-yl)carbamate 
• 1381761-97-2 1-((R)-1-((((3aR,4R,6R,6aR)-6-(6-amino-9H-purin-9-yl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methyl)(methyl)amino)-4-methylpentan-3-yl)-3-(4-(tert-butyl)phenyl)urea 

Relevant articles and documents

Resolution of α/β-amino acids by enantioselective penicillin G acylase from Achromobacter sp.

Penicillin G acylases (PGAs) are enantioselective enzymes catalyzing a hydrolysis of stable amide bond in a broad spectrum of substrates. Among them, derivatives of α- and β-amino acids represent a class of compounds with high application potential. PGAEc from Escherichia coli and PGAA from Achromobacter sp. CCM 4824 were used to catalyze enantioselective hydrolyses of seven selected N-phenylacetylated α/β-amino acid racemates. The PGAA showed higher stereoselectivity for enantiomers of N-PhAc-β-homoleucine, N-PhAc-α-tert-leucine and N-PhAc-β-leucine. To study the mechanism of enantiodiscrimination on molecular level, we have constructed a homology model of PGAA that was used in molecular docking experiments with the same substrates. In-silico experiments successfully reproduced the data from experimental enzymatic resolutions confirming validity of employed modeling protocol. We employed this protocol to evaluate enantiopreference of PGAA towards seven new substrates with application potential. For five of them, high enantioselectivity of PGAA was predicted.

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.

Experimental and theoretical studies on Mannich-type reactions of chiral non-racemic N-(benzyloxyethyl) nitrones

The nucleophilic addition of both silyl ketene acetals and lithium enolates derived from methyl acetate to chiral non-racemic N-(benzyloxyethyl)nitrones has been studied both experimentally and theoretically. Aromatic nitrones showed lower reactivity that

Kinetic and NMR spectroscopic studies of chiral mixed sodium/lithium amides used for the deprotonation of cyclohexene oxide

The mixed-metal complex formed from n-butylsodium, n-butyllithium, and a chiral amino ether has been studied by NMR spectroscopy. Three different mixed-metal amides were used as chiral bases for the deprotonation of cyclohexene oxide. The selectivity and initial rate of reaction were compared for sodium-amido ethers, lithium-amido ethers, and mixtures of sodium and lithiumamido ethers in diethyl ether and tetrahydrofuran, respectively. The mixed sodium/lithium amides are more reactive than the single sodium and lithium amides, whereas the stereoselectivities are higher when lithium amides are used. The alkali-metal/γ-amido ethers exhibit both higher initial reaction rates and stereoselectivities than their β-amido ether analogues. NMR spectroscopic studies of mixtures of n-butylsodium (nBuNa), n-butyllithium (nBuLi), and the γ-amino ethers in diethyl ether show the exclusive formation of dimeric mixed-metal amides. In diethyl ether, the lithium atom of the mixed-metal amide is internally coordinated and the sodium atom is exposed to solvent; however, in tetrahydrofuran, both metals are internally coordinated.

PROCESS FOR PRODUCING AMINO ACID DERIVATIVES

Process for producing amino acid derivatives, in which (a) an organic amine, the amino functionality of which is protected, or an α-amino acid, the amino functionality of which is protected, is subjected to an electrochemical reaction so as to form an ami

Chemoenzymatic synthesis of 4-amino-2-hydroxy acids: A comparison of mutant and wild-type oxidoreductases

We describe a new chemoenzymatic synthesis of enantiopure 4-amino-2-hydroxy acids using two biotransformations in a single-pot process in aqueous medium. These compounds are valuable as γ-turn mimics for investigations into the secondary structure of peptides. The enzyme substrates are a series of carbobenzyloxy (CBZ)-protected 4-amino-2-keto esters, prepared efficiently from the L-amino acids, alanine, leucine, phenylalanine, and valine. First, the α-amino acids were converted to the corresponding β-amino acids in a simple five-step procedure. A further one-carbon homologation via ozonolysis of the corresponding β-keto cyanophosphoranes gave the required α-keto esters in good yield. The enzyme catalyzed hydrolyses of all the α-keto esters to the corresponding α-keto acids proceeded smoothly with the lipase from Candida rugosa. Using the same reaction pot, it was found that wild-type lactate dehydrogenases from either Bacillus stearothermophilus CBS-LDH) or Staphylococcus epidermidis (SE-LDH) could be used to specifically reduce the ketone of the alanine-derived α-keto acid 2, giving the (S)- and CR)-2-hydroxy acids, respectively, in good yields. However, the more bulky α-keto acids 3, 4, and 5 (derived from valine, leucine, and phenylalanine) were not substrates for these enzymes. In contrast, the genetically engineered H205Q mutant of D-hydroxyisocaproate dehydrogenase proved to be an ideal catalyst for the reduction of all the α-keto acids 2-5, giving excellent yields of the CBZ-protected (2R,4S)-4-amino2-hydroxy acids as single diastereomers. This genetically engineered oxidoreductase has great potential value in synthesis due to its broad substrate specificity and high catalytic activity. For example, reduction of 1 mmol of N-protected (S)-4-amino-2-oxopentanoic acid 2 took just 4 h with the H205Q mutant giving, after esterification, the CR)-2-alcohol 25 in 85% yield, whereas with SE-LDH the reaction required 4 days to give a 67% yield of 25.

Enantioselektive Synthese von β-Aminosaeuren - TMS-SAMP als chirales Ammoniak-Aequivalent in der azaanalogen Michael-Addition an α,β-ungesaettigte Ester

Stichworte: Aminosaeuren * Asymmetrische Synthesen * Chirale Hilfsstoffe * Michael-Additionen

Stereochemistry of the Leucine 2,3-Aminomutase from Tissue Cultures of Andrographis paniculata

A leucine 2,3-aminomutase from Andrographis tissue cultures mediates the equilibrium between (2S)-α- and (3R)-β-leucine; the activity does not apparently depend on coenzyme B12.