13477-53-7

Basic information

• Product Name: 2-Hydroxy-4-amino butanoic acid
• Synonyms: ALPHA-HYDROXY-GAMMA-AMINOBUTANOIC ACID;ALPHA-HYDROXY-GAMMA-AMINO BUTYRIC ACID;2-HYDROXY-4-AMINOBUTANOIC ACID;2-HYDROXY-4-AMINO BUTYRIC ACID;2-hydroxy-4-aminobutanoicacid(haba);4-amino-2-hydroxy-butanoicaci;4-amino-2-hydroxy-butyricaci;4-amino-2-hydroxybutyricacid
• CAS NO: 13477-53-7
• Molecular Formula: C₄H₉NO₃
• Molecular Weight: 119.12
• EINECS: 1308068-626-2
• Product Categories: Alcohols and Derivatives;Amino Acids and Derivatives;(intermediate of amikacin sulfate)
• Mol File: 13477-53-7.mol

Chemical Properties

• Melting Point: 196-206°C
• Boiling Point: 361.8 °C at 760 mmHg
• Flash Point: 172.6 °C
• Appearance: /
• Density: 1.312 g/cm³
• Vapor Pressure: 1.08E-06mmHg at 25°C
• Refractive Index: 1.51
• PKA: 3.47±0.10(Predicted)
• CAS DataBase Reference: 2-Hydroxy-4-amino butanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Hydroxy-4-amino butanoic acid(13477-53-7)
• EPA Substance Registry System: 2-Hydroxy-4-amino butanoic acid(13477-53-7)

Safety Data

• Hazardous Substances Data: 13477-53-7(Hazardous Substances Data)

Usage

Uses

2-Hydroxy-4-amino Butanoic Acid is a GABA analog.

InChI:InChI=1/C4H9NO3/c5-2-1-3(6)4(7)8/h3,6H,1-2,5H2,(H,7,8)/t3-/m1/s1

Upstream product

• 1758-80-1 L-2,4-diaminobutyrate 
• 40732-91-0 γ-phthalimidoimino-α-hydroxybutyric acid 
• 40371-50-4 S-4-benzyloxycarbonylamino-2-hydroxybutyric acid 
• 56-12-2 4-amino-n-butyric acid 
• 3025-96-5 N-Acetyl-4-aminobutyric acid 
• 84658-40-2 2-hydroxy-glutaramic acid 
• 59712-12-8 4-amino-2-hydroxybutyraldehyde 
• 94891-74-4 O²,O³-diacetyl-L_g-tartaric acid ethyl ester-nitrile 
• 57229-74-0 (S)-2-hydroxysuccinamic acid 
• 57413-15-7 methyl 4-amino-2-hydroxybutanoate 

Downstream Products

• 34368-52-0 (S)-3-hydroxypyrrolidin-2-one 
• 40371-50-4 S-4-benzyloxycarbonylamino-2-hydroxybutyric acid 
• 188753-46-0 (S)-2-Hydroxy-4-(5-methyl-2-nitro-phenylamino)-butyric acid 
• 207305-60-0 (S)-4-[(tert-butoxycarbonyl)amino]-2-hydroxybutanoic acid 
• 850397-64-7 4-Benzyloxycarbonylamino-2S-hydroxy butyric acid ethyl ester 
• 149137-92-8 (2S)-4-(p-nitrobenzyloxycarbonyl)-amino-2-hydroxybutyric acid 
• 48172-10-7 (+)-(2S)-4-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-2-hydroxybutanoic acid 
• 1455088-71-7 (S)-4-(1-cyano-4-hydroxy-7-phenoxyisoquinoline-3-carboxamido)-2-hydroxybutanoic acid 
• 15166-68-4 3-hydroxy-2-pyrrolidinone 
• 43203-38-9 (SR)-2-Hydroxy-4-(benzylamino)-buttersaeure 
• 107-95-9 3-amino propanoic acid 
• 40732-91-0 γ-phthalimidoimino-α-hydroxybutyric acid 
• 54755-69-0 L-(-)-4-benzyloxycarbonylamino-2-hydroxybutyric acid 
• 1455086-97-1 2-(S)-hydroxy-4-[(4-hydroxy-7-phenoxyisoquinoline-3-carbonyl)amino]butyric acid 

Relevant articles and documents

α-Hydroxylation of Carboxylic Acids Catalyzed by Taurine Dioxygenase

Enzymes still have a limited application scope in synthetic organic chemistry. To expand this, different strategies exist that range from the de novo design of enzymes to the exploitation of the catalytic capabilities of known enzymes by converting different substrates; denoted as substrate promiscuity. We harnessed the synthetic potential offered by the taurine dioxygenase (TauD) from Escherichia coli (E. coli) by studying its promiscuous catalytic properties in the hydroxylation of carboxylic acid substrates. TauD showed high selectivities in the hydroxylation reaction but reduced levels of activity (26 % conversion, >96 % ee). We enhanced the enzyme substrate scope and improved the conversions for the tested substrates by introducing a point mutation at position 206 (F206Y). The conversions of the improved catalyst increased by at least 140 % compared to that of the wild-type enzyme. The number of carboxylic acids that accepted by the enzyme variant doubled from four to eight carboxylic acids.

Enantioselective Syntheses of (S)- and (R)-3-Hydroxypyrrolidin-2-ones via Lactate Dehydrogenase Catalysed Reductions of 4-Benzyloxycarbonylamino-2-oxobutanoic Acid

The first examples of the BS- and SE-lactate dehydrogenase catalysed reductions of an α-keto acid incorporating a nitrogen containing function in the side chain are described: (S)- and (R)-benzyloxycarbonylamino-2-hydroxybutanoic acids were prepared in good yield and excellent enantioselectivities and were converted to the (S)- and (R)-3-hydroxypyrrolidin-2-ones respectively.

Methoxyl kanamycin drug intermediate gamma-amino-alpha-hydroxybutyric acid synthesis method

A methoxyl kanamycin drug intermediate gamma-amino-alpha-hydroxybutyric acid synthesis method comprises the following steps: 21L of a sodium nitrate solution and 1.6 mol of a potassium bisulfite solution are added into a reaction vessel, stirring speed is controlled at 130-170rpm, the solution temperature is reduced to 3-5 DEG C, 9.6mol of cuprous chloride are added, 12.6mol of alpha-hydroxyl glutaramic acid are added in batches, 7.5-7.9mol of o-toluidine are added for reaction for 3-5h, then the solution temperature is raised to 60-65 DEG C for reaction for 5-6h, the solution temperature is reduced to 10-15 DEG C, an oxalic acid solution is added to adjust the pH to 2-3, the solution temperature is reduced to 5-8 DEG C for precipitation of a crystal, and the crystal is filtered, washed with acetonitrile, washed with ethyl acetate, dehydrated with a dehydrating agent, and recrystallized in nitromethane to obtain crystal gamma-amino-alpha-hydroxybutyric acid.

Structural and functional characterization of plant aminoaldehyde dehydrogenase from pisum sativum with a broad specificity for natural and synthetic aminoaldehydes

Aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19) belong to the large aldehyde dehydrogenase (ALDH) superfamily, namely, the ALDH9 family. They oxidize polyamine-derived ω-aminoaldehydes to the corresponding ω-amino acids. Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with β-nicotinamide adenine dinucleotide (NAD+) at 2.4 and 2.15 A resolution, respectively. Both recombinant proteins are dimeric and, similarly to other ALDHs, each monomer is composed of an oligomerization domain, a coenzyme binding domain and a catalytic domain. Each subunit binds NAD+ as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD+ binding site. While the NAD+ binding mode is classical for PsAMADH2, that for PsAMADH1 is unusual among ALDHs. A glycerol molecule occupies the substrate binding site and mimics a bound substrate. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into γ-butyrobetaine, which is the carnitine precursor in animal cells. This activity highly suggests that in addition to their contribution to the formation of compatible osmolytes such as glycine betaine, β-alanine betaine and γ-aminobutyric acid, AMADHs might participate in carnitine biosynthesis in plants.

Process for the production of omega-amino-alpha-hydroxycarboxylic acid

An optically active ω-amino-α-hydroxycarboxylic acid of the formula: wherein n is 1 or 2, which process comprises reacting an ω-ester of an α-amino acid with nitrous acid under an acidic condition to convert an amino group to an hydroxy group to obtain an ω-alkoxycarbonyl-α-hydroxycarboxylic acid, reacting the ω-alkoxycarbonyl-α-hydroxycarboxylic acid with ammonia to convert an alkoxycarbonyl group to an amide group to obtain an ω-aminocarbonyl-α-hydroxycarboxylic acid, and reacting the ω-aminocarbonyl-α-hydroxycarboxylic acid with an active halogen to convert the amido group to an amino group.

Hydroxylations microbiologiques de pyrrolidinones-2 (note de laboratoire)

Microbial hydroxylations of various pyrrolidin-2 ones, especially N-acylated, with Beauveria sulfurescens have been carried out.The regioselectivity depends on the nature of the substituent on the nitrogen atom and the hydroxylation may occur at position 3,4 or 5 of the heterocycle.Hydroxylations at position 3 or 4 occur with low enantioselectivity.

OXIDATIVE DEGRADATION OF β- AND γ-AMINO ACIDS BY CONTACT GLOW DISCHARGE ELECTROLYSIS

The degradation of β- and γ-amino acids in aqueous solutions by contact glow discharge electrolysis (CGDE) was studied.It was found that the reaction is actually a stepwise oxidative degradation by hydroxyl radical produced by CGDE.