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80126-52-9

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80126-52-9 Usage

General Description

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 chemical has potential applications in the fields of medicine and biochemistry, including as a tool for studying protein structure and function, as well as a potential therapeutic agent for the treatment of certain diseases. D-3-Chlorophenylalanine may also be used in the synthesis of novel pharmaceuticals and in the development of new chemical reactions. Its unique structural features make it a valuable building block for the preparation of diverse compounds with varied biological activities.

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.

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.

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