2361-98-0

Basic information

• Product Name: butyl 2-acetylamino-3-phenylpropanoate
• Synonyms: butyl 2-acetylamino-3-phenylpropanoate
• CAS NO: 2361-98-0
• Molecular Weight: 263.337
• Mol File: 2361-98-0.mol
• Article Data: 5

Chemical Properties

• CAS DataBase Reference: butyl 2-acetylamino-3-phenylpropanoate(CAS DataBase Reference)
• NIST Chemistry Reference: butyl 2-acetylamino-3-phenylpropanoate(2361-98-0)
• EPA Substance Registry System: butyl 2-acetylamino-3-phenylpropanoate(2361-98-0)

Safety Data

• Hazardous Substances Data: 2361-98-0(Hazardous Substances Data)

Upstream product

• 2361-96-8 ethyl N-acetyl-(L)-phenylalaninate 
• 71-36-3 butan-1-ol 
• 27172-85-6 phenylalanine methyl ester hydrochloride 
• 100-39-0 benzyl bromide 
• 100-44-7 benzyl chloride 
• 21132-20-7 (RS)-ethyl-2-acetamido-2-cyano-3-phenylpropanoate 
• 109-21-7 butyl butyrate 
• 1575605-52-5 allyl 2-acetylamino-3-phenylpropanoate 
• 21156-62-7 N-acetylphenylalanine methyl ester 
• 5619-07-8 methyl 2-amino-3-phenylpropanoate hydrochloride 
• 112667-58-0 (E)-2-Acetylamino-3-phenyl-acrylic acid butyl ester 

Relevant articles and documents

ASYMMETRIC HYDROGENATION IN THE PRESENCE OF BISDIPHENYLPHOSPHINE COMPLEXES OF RHODIUM. 3. MOLECULAR STRUCTURE OF 2R-3-PHENYL-2-(N-METHYLDIPHENYLPHOSPHINAMINO)-1-DIPHENYLPHOSPHINOXYPROPANE(1,5-CYCLOOCTADIENE)RHODIUM(I) PERCHLORATE AND ITS EFFECTIVENESS AS AN ENANTIOSELECTIVE CATALYST

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Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting

Bioimprinting is a technique in which an aqueous solution of a protein molecule along with the imprint molecule is dried to remove bulk water. Subtilisin was dissolved in an aqueous buffer with a substrate analog and precipitated with the substrate alcoho

Homogeneous enzymatic reactions in ionic liquids with poly(ethylene glycol)-modified subtilisin

Subtilisin Carlsberg was covalently modified with comb-shaped poly(ethylene glycol) (PM13). PM13-modified subtilisin (PM 13-Sub) was readily solubilized in three different ionic liquids (ILs), i.e., [Emim][Tf2N], [C2OC1mim][Tf 2N] and [C2OHmim][Tf2N]. Analysis of homogeneous enzymatic reactions in the ILs revealed that PM13-Sub exhibited excellent catalytic performance while the native enzyme suspended in ILs showed no activity. Hydrophobicity of ILs slightly affected enzyme activity, and the relatively hydrophobic IL [Emim][Tf2N] was the preferred medium for enzymatic reactions, similar to enzymatic reactions in conventional organic solvents. Enzyme activity was much higher in [Emim][Tf2N] than in conventional organic solvents, and excellent activity was associated with unique properties of ILs such as hydrophobicity and high polarity. Furthermore, PM13-Sub showed good stability in [Emim][Tf 2N], and maintained 80% of its initial activity after 60 h. The Royal Society of Chemistry 2006.