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(E,2S)-2-amino-5-phenyl-pent-4-enoic acid is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

52161-76-9

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52161-76-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 52161-76-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,2,1,6 and 1 respectively; the second part has 2 digits, 7 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 52161-76:
(7*5)+(6*2)+(5*1)+(4*6)+(3*1)+(2*7)+(1*6)=99
99 % 10 = 9
So 52161-76-9 is a valid CAS Registry Number.

52161-76-9SDS

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 (E,2S)-2-amino-5-phenyl-pent-4-enoic acid

1.2 Other means of identification

Product number -
Other names (S)-trans-cinnamylglycine

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:52161-76-9 SDS

52161-76-9Relevant academic research and scientific papers

Tailored Mutants of Phenylalanine Ammonia-Lyase from Petroselinum crispum for the Synthesis of Bulky l- and d-Arylalanines

Filip, Alina,Nagy, Emma Z. A.,Tork, Souad D.,Bánóczi, Gergely,To?a, Monica I.,Irimie, Florin D.,Poppe, László,Paizs, Csaba,Bencze, László C.

, p. 2627 - 2633 (2018/05/03)

Tailored mutants of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) were created and tested in ammonia elimination from various sterically demanding, non-natural analogues of phenylalanine and in ammonia addition reactions into the corresponding (E)-arylacrylates. The wild-type PcPAL was inert or exhibited quite poor conversions in both reactions with all members of the substrate panel. Appropriate single mutations of residue F137 and the highly conserved residue I460 resulted in PcPAL variants that were active in ammonia elimination but still had a poor activity in ammonia addition onto bulky substrates. However, combined mutations that involve I460 besides the well-studied F137 led to mutants that exhibited activity in ammonia addition as well. The synergistic multiple mutations resulted in substantial substrate scope extension of PcPAL and opened up new biocatalytic routes for the synthesis of both enantiomers of valuable phenylalanine analogues, such as (4-methoxyphenyl)-, (napthalen-2-yl)-, ([1,1′-biphenyl]-4-yl)-, (4′-fluoro-[1,1′-biphenyl]-4-yl)-, and (5-phenylthiophene-2-yl)alanines.

Synthesis of Optically Pure (S, E)-2-Amino-5-arylpent-4-enoic Acids by Heck Reactions of Nickel Complexes

Parpart, Silvio,Mardiyan, Zorayr Z.,Ehlers, Peter,Petrosyan, Andranik,Mkrtchyan, Anna F.,Saghyan, Ashot S.,Langer, Peter

supporting information, p. 793 - 798 (2018/01/27)

Starting from commercially available building blocks a variety of enantiomerically pure (S)-2-amino-4-enoic acids has been synthesized by the Heck reaction using Ni-(S)-BPB {Nickel- N -[(S)-benzylprolyl]aminobenzophenone} as a chiral auxiliary. The reactions proceeded in very good yields and with high E -selectivity.

Convenient, large-scale asymmetric synthesis of enantiomerically pure trans-cinnamylglycine and -α-alanine

Qiu, Wei,Soloshonok, Vadim A.,Cai, Chaozhong,Tang, Xuejun,Hruby, Victor J.

, p. 2577 - 2582 (2007/10/03)

Asymmetric syntheses of (S)-trans-cinnamylglycine and (S)-α-trans- cinnamyl-α-alanine via reactions of cinnamyl halides (Cl, Br) with Ni(II)- complexes of the chiral Schiff base of glycine or alanine with (S)-o-[N-(N- benzylprolyl)amino]benzophenone were

Kinetic Resolution of Unnatural and Rarely Occuring Amino Acids: Enantioselective Hydrolysis of N-Acyl Amino Acids Catalyzed by Acylase I

Chenault, H. Keith,Dahmer, Juergen,Whitesides, George M.

, p. 6354 - 6364 (2007/10/02)

Acylase I (aminoacylase; N-acylamino-acid amidohydrolase, EC 3.5.1.14, from porcine kidney and the fungus Aspergillus) is broadly applicable enzymatic catalyst for the kinetic resolution of unnatural and rarely occuring α-amino acids.Its enantioselectivity for the hydrolysis of N-acyl L-α-amino acids is nearly absolute, yet it accepts substrates having a wide range of structure and functionality.This paper reports the initial rates of enzyme-catalyzed hydrolysis of over 50 N-acyl amino acids and analogues, the stabilities of the enzymes in aqueous and aqueous/organic solutions, and the effects of different acyl groups and metal ions on the rates of enzymatic hydrolysis.Eleven α-amino and α-methyl α-amino acids were resolved on a 2-29-g scale.Crude L- and D-amino acid products had generally >90percent ee.The utility of resolved amino acids as chiral synthons was illustrated by the preparation of (R)- and (S)-1-butene oxide and the diastereoselective (cis:trans, 7-8:1) iodolactonization of three 2-amino-4-alkenoic acid derivatives.

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