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EC 4.3.1.5

Base Information
  • Chemical Name:EC 4.3.1.5
  • CAS No.:9024-28-6
  • Molecular Formula:
  • Molecular Weight:0
  • Hs Code.:
EC 4.3.1.5

Synonyms:(S)-Phenylalanineammonia lyase; E.C. 4.3.1.24; E.C. 4.3.1.5; L-Phenylalanine ammonia-lyase; PAL;Phenylalanine ammonia-lyase; Phenylalanine ammonium-lyase; Phenylalaninedeaminase

Suppliers and Price of EC 4.3.1.5
Supply Marketing:
Business phase:
The product has achieved commercial mass production*data from LookChem market partment
Manufacturers and distributors:
  • Manufacture/Brand
  • Chemicals and raw materials
  • Packaging
  • price
  • Sigma-Aldrich
  • Phenylalanine Ammonia-Lyase from Rhodotorula glutinis Grade I, buffered aqueous glycerol solution, 0.8-2.0?units/mg protein
  • 2 units
  • $ 150.00
  • Sigma-Aldrich
  • Phenylalanine Ammonia-Lyase from Rhodotorula glutinis Grade I, buffered aqueous glycerol solution, 0.8-2.0 units/mg protein
  • 2un
  • $ 145.00
  • Sigma-Aldrich
  • Phenylalanine Ammonia-Lyase from Rhodotorula glutinis Grade I, buffered aqueous glycerol solution, 0.8-2.0?units/mg protein
  • 10 units
  • $ 539.00
  • Sigma-Aldrich
  • Phenylalanine Ammonia-Lyase from Rhodotorula glutinis Grade I, buffered aqueous glycerol solution, 0.8-2.0 units/mg protein
  • 10un
  • $ 519.00
  • American Custom Chemicals Corporation
  • L-PHENYLALANINE AMMONIA-LYASE 95.00%
  • 5MG
  • $ 498.48
Total 5 raw suppliers
Chemical Property of EC 4.3.1.5
Chemical Property:
  • Storage Temp.:−20°C 
Purity/Quality:

99%, *data from raw suppliers

Phenylalanine Ammonia-Lyase from Rhodotorula glutinis Grade I, buffered aqueous glycerol solution, 0.8-2.0?units/mg protein *data from reagent suppliers

Safty Information:
  • Pictogram(s):  
  • Hazard Codes: 
  • Safety Statements: 24/25 
MSDS Files:
Useful:
  • General Description EC 4.3.1.5, also known as phenylalanine ammonia-lyase (PAL), is an enzyme that catalyzes the deamination of L-phenylalanine to form trans-cinnamic acid and ammonia. This study demonstrates that PAL exhibits substrate versatility by efficiently processing novel synthetic analogs, such as 2-amino-3-(5-phenylfuran-2-yl)propionic acids and 5-phenylfuran-2-ylacrylic acids, into their respective enantiomers through reversible biocatalytic reactions. The enzyme's ability to resolve racemic mixtures highlights its potential for chiral synthesis and biotechnological applications.
Refernces

2-amino-3-(5-phenylfuran-2-yl)propionic acids and 5-phenylfuran-2-ylacrylic acids are novel substrates of phenylalanine ammonia-lyase

10.3987/COM-10-S(E)60

The research focused on the synthesis and characterization of 2-amino-3-(5-phenylfuran-2-yl)propionic acids and 5-phenylfuran-2-ylacrylic acids, which were found to be novel substrates for phenylalanine ammonia-lyase (PAL). The purpose of the study was to explore the enzyme's ability to catalyze the conversion of these compounds and to isolate their D- and L-enantiomers. The researchers synthesized the compounds and characterized them using various spectroscopic techniques. They then used recombinant PAL to convert the racemic mixtures into their corresponding acrylates, from which the D-enantiomers were isolated. Conversely, L-enantiomers were prepared by reversing the PAL reaction in the presence of 6 M ammonia at pH 10. The study concluded that these new compounds are good substrates for recombinant PAL and can be resolved into their enantiomers through biocatalysis. The chemicals used in the process included various anilines, furan-2-carbaldehyde, triphenyl-λ5-phosphanilidene acetic acid ethyl ester, and other reagents and solvents for the synthesis and characterization of the novel furanylalanines.

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