14091-11-3 Usage
Description
2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID, also known as 2-Chloro-DL-phenylalanine, is an organic compound derived from the amino acid phenylalanine with a chlorine atom substitution at the 2nd position of the phenyl ring. It is characterized by its unique chemical structure, which contributes to its specific properties and potential applications in various fields.
Uses
Used in Chemical Synthesis:
2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID is used as a key intermediate in the synthesis of various organic compounds, particularly for the production of 2-benzylpyrroles and 2-benzoylpyrroles. These synthesized compounds exhibit insecticidal and acaricidal activity, making them valuable for agricultural and pest control applications.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID is utilized as a building block for the development of new drugs with potential therapeutic applications. Its unique structure allows for the creation of novel molecules with specific biological activities, contributing to the advancement of medicinal chemistry.
Used in Agrochemical Industry:
2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID is used as a starting material for the development of agrochemicals, specifically insecticides and acaricides. Its incorporation into these chemical products enhances their effectiveness in controlling pests and parasites, thereby improving crop protection and yield.
Used in Research and Development:
In the field of research and development, 2-AMINO-3-(2-CHLORO-PHENYL)-PROPIONIC ACID serves as an important compound for studying the structure-activity relationships of various biologically active molecules. Its unique properties make it a valuable tool for understanding the mechanisms of action and potential applications of related compounds in different industries.
Check Digit Verification of cas no
The CAS Registry Mumber 14091-11-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,0,9 and 1 respectively; the second part has 2 digits, 1 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 14091-11:
(7*1)+(6*4)+(5*0)+(4*9)+(3*1)+(2*1)+(1*1)=73
73 % 10 = 3
So 14091-11-3 is a valid CAS Registry Number.
InChI:InChI=1/C9H10ClNO2/c10-9(11,8(12)13)6-7-4-2-1-3-5-7/h1-5H,6,11H2,(H,12,13)/t9-/m0/s1
14091-11-3Relevant articles and documents
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Nevenzel,Shelberg,Niemann
, p. 3024 (1949)
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Phenylalanine ammonia lyase catalyzed synthesis of amino acids by an MIO-cofactor independent pathway
Lovelock, Sarah L.,Lloyd, Richard C.,Turner, Nicholas J.
, p. 4652 - 4656 (2014/05/20)
Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E1cB elimination mechanism. All manner of things: A competing MIO-independent (MIO=4-methylideneimidazole-5-one) reaction pathway has been identified for phenylalanine ammonia lyases (PALs), which proceeds in a non-stereoselective manner, resulting in the generation of D-phenylalanine derivatives. The mechanism of D-amino acid formation is explored through isotopic-labeling studies and mutagenesis of key active-site residues.
Enantioselective synthesis of non-natural amino acids using phenylalanine dehydrogenases modified by site-directed mutagenesis
Busca, Patricia,Paradisi, Francesca,Moynihan, Eamonn,Maguire, Anita R.,Engel, Paul C.
, p. 2684 - 2691 (2007/10/03)
The substrate scope of three mutants of phenylalanine dehydrogenase as biocatalysts for the transformation of a series of 2-oxo acids, structurally related to phenylpyruvic acid, to the analogous -amino acids, non-natural analogues of phenylalanine, has been investigated. The mutant enzymes are more tolerant than the wild type enzyme of the non-natural substrates, especially those with substituents at the 4-position on the phenyl ring. Excellent enantiocontrol resulted in all cases.