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D-3-Chlorophenylalanine is a chemical compound that belongs to the class of phenylalanine derivatives. It is an amino acid derivative containing a chlorine atom at the 3-position of the phenyl ring. This unique structural feature endows it with potential applications in various fields, including medicine and biochemistry.

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  • 80126-52-9 Structure
  • Basic information

    1. Product Name: D-3-Chlorophenylalanine
    2. Synonyms: D-Phe(3-Cl)-OH;3-(3-Chlorophenyl)-D-alanine;3-CHLORO-D-PHENYLALANINEHCL 99+%;H-D-Phe(3-Cl)-OH*HCl;3-Chloro-D-phenylalanine HCl D-3-Chlorophe;D-3-Chloro-phe-OH;3-Chloro-D-phenylala;D-Phe(3-Cl)-OH 3-Chloro-D-Phenylalanine
    3. CAS NO:80126-52-9
    4. Molecular Formula: C9H10ClNO2
    5. Molecular Weight: 199.63
    6. EINECS: N/A
    7. Product Categories: Phenylalanine [Phe, F];Unusual Amino Acids;Peptide;a-amino;Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids
    8. Mol File: 80126-52-9.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: 339.5 °C at 760 mmHg
    3. Flash Point: 159.1 °C
    4. Appearance: White/Powder
    5. Density: 1.336 g/cm3
    6. Refractive Index: N/A
    7. Storage Temp.: Store at 0°C
    8. Solubility: N/A
    9. PKA: 2.17±0.10(Predicted)
    10. CAS DataBase Reference: D-3-Chlorophenylalanine(CAS DataBase Reference)
    11. NIST Chemistry Reference: D-3-Chlorophenylalanine(80126-52-9)
    12. EPA Substance Registry System: D-3-Chlorophenylalanine(80126-52-9)
  • Safety Data

    1. Hazard Codes: Xi
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 80126-52-9(Hazardous Substances Data)

80126-52-9 Usage

Uses

Used in Pharmaceutical Research:
D-3-Chlorophenylalanine is used as a research tool for studying protein structure and function. Its incorporation into proteins can provide insights into the role of specific amino acid residues in protein folding, stability, and interactions.
Used in Drug Development:
D-3-Chlorophenylalanine is used as a potential therapeutic agent for the treatment of certain diseases. Its unique chemical properties may offer new avenues for the development of targeted therapies, particularly in the treatment of neurological disorders and cancer.
Used in Synthesis of Novel Pharmaceuticals:
D-3-Chlorophenylalanine is used as a building block in the synthesis of novel pharmaceuticals. Its unique structural features allow for the preparation of diverse compounds with varied biological activities, potentially leading to the discovery of new drugs with improved efficacy and selectivity.
Used in Development of New Chemical Reactions:
D-3-Chlorophenylalanine is used in the development of new chemical reactions. Its reactivity and unique structural features can be exploited to design innovative synthetic routes, expanding the scope of organic chemistry and enabling the synthesis of complex molecules with potential applications in various fields.

Check Digit Verification of cas no

The CAS Registry Mumber 80126-52-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,0,1,2 and 6 respectively; the second part has 2 digits, 5 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 80126-52:
(7*8)+(6*0)+(5*1)+(4*2)+(3*6)+(2*5)+(1*2)=99
99 % 10 = 9
So 80126-52-9 is a valid CAS Registry Number.

80126-52-9 Well-known Company Product Price

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  • Alfa Aesar

  • (H63239)  3-Chloro-D-phenylalanine, 98%   

  • 80126-52-9

  • 250mg

  • 355.0CNY

  • Detail
  • Alfa Aesar

  • (H63239)  3-Chloro-D-phenylalanine, 98%   

  • 80126-52-9

  • 1g

  • 1065.0CNY

  • Detail
  • Alfa Aesar

  • (H63239)  3-Chloro-D-phenylalanine, 98%   

  • 80126-52-9

  • 5g

  • 4260.0CNY

  • Detail

80126-52-9SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name (R)-2-Amino-3-(3-chlorophenyl)propanoic acid

1.2 Other means of identification

Product number -
Other names (2R)-2-amino-3-(3-chlorophenyl)propanoic acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:80126-52-9 SDS

80126-52-9Relevant articles and documents

A novel phenylalanine ammonia-lyase from Pseudozyma antarctica for stereoselective biotransformations of unnatural amino acids

Varga, Andrea,Csuka, Pál,Sonesouphap, Orlavanah,Bánóczi, Gergely,To?a, Monica Ioana,Katona, Gabriel,Molnár, Zsófia,Bencze, László Csaba,Poppe, László,Paizs, Csaba

, p. 185 - 194 (2020/04/28)

A novel phenylalanine ammonia-lyase of the psychrophilic yeast Pseudozyma antarctica (PzaPAL) was identified by screening microbial genomes against known PAL sequences. PzaPAL has a significantly different substrate binding pocket with an extended loop (26 aa long) connected to the aromatic ring binding region of the active site as compared to the known PALs from eukaryotes. The general properties of recombinant PzaPAL expressed in E. coli were characterized including kinetic features of this novel PAL with L-phenylalanine (S)-1a and further racemic substituted phenylalanines rac-1b-g,k. In most cases, PzaPAL revealed significantly higher turnover numbers than the PAL from Petroselinum crispum (PcPAL). Finally, the biocatalytic performance of PzaPAL and PcPAL was compared in the kinetic resolutions of racemic phenylalanine derivatives (rac-1a-s) by enzymatic ammonia elimination and also in the enantiotope selective ammonia addition reactions to cinnamic acid derivatives (2a-s). The enantiotope selectivity of PzaPAL with o-, m-, p-fluoro-, o-, p-chloro- and o-, m-bromo-substituted cinnamic acids proved to be higher than that of PcPAL.

Bi-enzymatic Conversion of Cinnamic Acids to 2-Arylethylamines

Weise, Nicholas J.,Thapa, Prasansa,Ahmed, Syed T.,Heath, Rachel S.,Parmeggiani, Fabio,Turner, Nicholas J.,Flitsch, Sabine L.

, p. 995 - 998 (2020/01/21)

The conversion of carboxylic acids, such as acrylic acids, to amines is a transformation that remains challenging in synthetic organic chemistry. Despite the ubiquity of similar moieties in natural metabolic pathways, biocatalytic routes seem to have been overlooked for this purpose. Herein we present the conception and optimisation of a two-enzyme system, allowing the synthesis of β-phenylethylamine derivatives from readily-available ring-substituted cinnamic acids. After characterisation of both parts of the reaction in a two-step approach, a set of conditions allowing the one-pot biotransformation was optimised. This combination of a reversible deaminating and irreversible decarboxylating enzyme, both specific for the amino acid intermediate in tandem, represents a general method by which new strategies for the conversion of carboxylic acids to amines could be designed.

Highly selective synthesis of d-amino acids from readily available l-amino acids by a one-pot biocatalytic stereoinversion cascade

Zhang, Danping,Jing, Xiaoran,Zhang, Wenli,Nie, Yao,Xu, Yan

, p. 29927 - 29935 (2019/10/01)

d-Amino acids are key intermediates required for the synthesis of important pharmaceuticals. However, establishing a universal enzymatic method for the general synthesis of d-amino acids from cheap and readily available precursors with few by-products is challenging. In this study, we constructed and optimized a cascade enzymatic route involving l-amino acid deaminase and d-amino acid dehydrogenase for the biocatalytic stereoinversions of l-amino acids into d-amino acids. Using l-phenylalanine (l-Phe) as a model substrate, this artificial biocatalytic cascade stereoinversion route first deaminates l-Phe to phenylpyruvic acid (PPA) through catalysis involving recombinant Escherichia coli cells that express l-amino acid deaminase from Proteus mirabilis (PmLAAD), followed by stereoselective reductive amination with recombinant meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum (StDAPDH) to produce d-phenylalanine (d-Phe). By incorporating a formate dehydrogenase-based NADPH-recycling system, d-Phe was obtained in quantitative yield with an enantiomeric excess greater than 99%. In addition, the cascade reaction system was also used to stereoinvert a variety of aromatic and aliphatic l-amino acids to the corresponding d-amino acids by combining the PmLAAD whole-cell biocatalyst with the StDAPDH variant. Hence, this method represents a concise and efficient route for the asymmetric synthesis of d-amino acids from the corresponding l-amino acids.

Engineered Aminotransferase for the Production of d-Phenylalanine Derivatives Using Biocatalytic Cascades

Walton, Curtis J. W.,Parmeggiani, Fabio,Barber, Janet E. B.,McCann, Jenna L.,Turner, Nicholas J.,Chica, Roberto A.

, p. 470 - 474 (2017/12/15)

d-Phenylalanine derivatives are valuable chiral building blocks for a wide range of pharmaceuticals. Here, we developed stereoinversion and deracemization biocatalytic cascades to synthesize d-phenylalanine derivatives that contain electron-donating or -withdrawing substituents of various sizes and at different positions on the phenyl ring with a high enantiomeric excess (90 to >99 % ee) from commercially available racemic mixtures or l-amino acids. These whole-cell systems couple Proteus mirabilis l-amino acid deaminase with an engineered aminotransferase that displays native-like activity towards d-phenylalanine, which we generated from Bacillus sp. YM-1 d-amino acid aminotransferase. Our cascades are applicable to preparative-scale synthesis and do not require cofactor-regeneration systems or chemical reducing agents.

Organocatalytic Enantioselective Addition of α-Aminoalkyl Radicals to Isoquinolines

Liu, Xiangyuan,Liu, Yang,Chai, Guobi,Qiao, Baokun,Zhao, Xiaowei,Jiang, Zhiyong

supporting information, p. 6298 - 6301 (2018/10/09)

With a dual organocatalytic system involving a chiral phosphoric acid and a dicyanopyrazine-derived chromophore (DPZ) photosensitizer and under the irradiation with visible light, an enantioselective Minisci-type addition of α-amino acid-derived redox-active esters (RAEs) to isoquinolines has been developed. A variety of prochiral α-aminoalkyl radicals generated from RAEs were successfully introduced on isoquinolines, providing a range of valuable α-isoquinoline-substituted chiral secondary amines in high yields with good to excellent enantioselectivities.

Influence of the aromatic moiety in α- And β-arylalanines on their biotransformation with phenylalanine 2,3-aminomutase from: Pantoea agglomerans

Varga, Andrea,Bánóczi, Gergely,Nagy, Botond,Bencze, László Csaba,To?a, Monica Ioana,Gellért, ákos,Irimie, Florin Dan,Rétey, János,Poppe, László,Paizs, Csaba

, p. 56412 - 56420 (2016/07/06)

In this study enantiomer selective isomerization of various racemic α- and β-arylalanines catalysed by phenylalanine 2,3-aminomutase from Pantoea agglomerans (PaPAM) was investigated. Both α- and β-arylalanines were accepted as substrates when the aryl moiety was relatively small, like phenyl, 2-, 3-, 4-fluorophenyl or thiophen-2-yl. While 2-substituted α-phenylalanines bearing bulky electron withdrawing substituents did not react, the corresponding substituted β-aryl analogues were converted rapidly. Conversion of 3- and 4-substituted α-arylalanines happened smoothly, while conversion of the corresponding β-arylalanines was poor or non-existent. In the range of pH 7-9 there was no significant influence on the conversion of racemic α- or β-(thiophen-2-yl)alanines, whereas increasing the concentration of ammonia (ammonium carbonate from 50 to 1000 mM) inhibited the isomerization progressively and decreased the amount of the by-product (i.e. (E)-3-(thiophen-2-yl)acrylic acid was detected). In all cases, the high ee values of the products indicated excellent enantiomer selectivity and stereospecificity of the isomerization except for (S)-2-nitro-α-phenylalanine (ee 92%) from the β-isomer. Substituent effects were rationalized by computational modelling revealing that one of the main factors controlling biocatalytic activity was the energy difference between the covalent regioisomeric enzyme-substrate complexes.

Telescopic one-pot condensation-hydroamination strategy for the synthesis of optically pure L-phenylalanines from benzaldehydes

Parmeggiani, Fabio,Ahmed, Syed T.,Weise, Nicholas J.,Turner, Nicholas J.

, p. 7256 - 7262 (2016/10/26)

A chemo-enzymatic telescopic approach was designed for the synthesis of L-arylalanines in high yield and optical purity, starting from commercially available and inexpensive substituted benzaldehydes. The method exploits a chemical Knoevenagel–Doebner condensation (optimised to give complete conversions in a short reaction time, employing microwave irradiation) and a biocatalytic phenylalanine ammonia lyase mediated hydroamination (for the stereoselective addition of ammonia). The two reactions can be run sequentially in one pot, bringing together the advantages of chemical and biological catalysis. The preparative applicability was demonstrated with the synthesis of five L-dihalophenylalanines (71–84% yield, 98–99% ee) of relevance as molecular probes, for medicinal chemistry and for the synthesis of pharmaceutical ingredients.

Intensified biocatalytic production of enantiomerically pure halophenylalanines from acrylic acids using ammonium carbamate as the ammonia source

Weise, Nicholas J.,Ahmed, Syed T.,Parmeggiani, Fabio,Siirola, Elina,Pushpanath, Ahir,Schell, Ursula,Turner, Nicholas J.

, p. 4086 - 4089 (2016/07/06)

An intensified, industrially-relevant strategy for the production of enantiopure halophenylalanines has been developed using the novel combination of a cyanobacterial phenylalanine ammonia lyase (PAL) and ammonium carbamate reaction buffer. The process boasts STYs up to >200 g L-1 d-1, ees ≥ 98% and simplified catalyst/reaction buffer preparation and work up.

The bacterial ammonia lyase EncP: A tunable biocatalyst for the synthesis of unnatural amino acids

Weise, Nicholas J.,Parmeggiani, Fabio,Ahmed, Syed T.,Turner, Nicholas J.

supporting information, p. 12977 - 12983 (2015/10/28)

Enzymes of the class I lyase-like family catalyze the asymmetric addition of ammonia to arylacrylates, yielding high value amino acids as products. Recent examples include the use of phenylalanine ammonia lyases (PALs), either alone or as a gateway to deracemization cascades (giving (S)- or (R)-α-phenylalanine derivatives, respectively), and also eukaryotic phenylalanine aminomutases (PAMs) for the synthesis of the (R)-β-products. Herein, we present the investigation of another family member, EncP from Streptomyces maritimus, thereby expanding the biocatalytic toolbox and enabling the production of the missing (S)-β-isomer. EncP was found to convert a range of arylacrylates to a mixture of (S)-α- and (S)-β-arylalanines, with regioselectivity correlating to the strength of electron-withdrawing/-donating groups on the ring of each substrate. The low regioselectivity of the wild-type enzyme was addressed via structure-based rational design to generate three variants with altered preference for either α- or β-products. By examining various biocatalyst/substrate combinations, it was demonstrated that the amination pattern of the reaction could be tuned to achieve selectivities between 99:1 and 1:99 for β:α-product ratios as desired.

Synthesis of D- and L-Phenylalanine Derivatives by Phenylalanine Ammonia Lyases: A Multienzymatic Cascade Process

Parmeggiani, Fabio,Lovelock, Sarah L.,Weise, Nicholas J.,Ahmed, Syed T.,Turner, Nicholas J.

, p. 4608 - 4611 (2015/04/14)

The synthesis of substituted D-phenylalanines in high yield and excellent optical purity, starting from inexpensive cinnamic acids, has been achieved with a novel one-pot approach by coupling phenylalanine ammonia lyase (PAL) amination with a chemoenzymatic deracemization (based on stereoselective oxidation and nonselective reduction). A simple high-throughput solid-phase screening method has also been developed to identify PALs with higher rates of formation of non-natural D-phenylalanines. The best variants were exploited in the chemoenzymatic cascade, thus increasing the yield and ee value of the D-configured product. Furthermore, the system was extended to the preparation of those L-phenylalanines which are obtained with a low ee value using PAL amination.

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