34271-27-7

Basic information

• Product Name: Acetyl-D-2-aminobutyric acid
• Synonyms: Acetyl-D-α-aminobutyric acid;Acetyl-D-α-aminobutyric acid≥ 99% (HPLC);Acetyl-D-2-aminobutyric acid;Nsc203440;(R)-2-AcetaMidobutanoic acid;D-2-(Acetamido)butyric acid
• CAS NO: 34271-27-7
• Molecular Formula: C₆H₁₁NO₃
• Molecular Weight: 145.15644
• Mol File: 34271-27-7.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 368.2°C at 760 mmHg
• Flash Point: 176.5°C
• Appearance: /
• Density: 1.129g/cm³
• Vapor Pressure: 1.97E-06mmHg at 25°C
• Refractive Index: 1.456
• Storage Temp.: Sealed in dry,Room Temperature
• CAS DataBase Reference: Acetyl-D-2-aminobutyric acid(CAS DataBase Reference)
• NIST Chemistry Reference: Acetyl-D-2-aminobutyric acid(34271-27-7)
• EPA Substance Registry System: Acetyl-D-2-aminobutyric acid(34271-27-7)

Safety Data

• Hazardous Substances Data: 34271-27-7(Hazardous Substances Data)

Usage

Chemical Properties

White powder

InChI:InChI=1/C6H11NO3/c1-3-5(6(9)10)7-4(2)8/h5H,3H2,1-2H3,(H,7,8)(H,9,10)

Upstream product

• 65499-61-8 (Z)-α-N-acetylamino-2-butenoic acid 
• 62973-41-5 2-(N-Acetylamino-)-buttersaeureethylester 
• 7211-57-6 2-(acetylamino)butanoic acid 
• 2623-91-8 (R)-2-aminobutyric acid 
• 108-24-7 acetic anhydride 

Downstream Products

• 2623-91-8 (R)-2-aminobutyric acid 
• 1492-24-6 L-2-aminobutyric acid 

Relevant articles and documents

L-Methionine related 1-amino acids by acylase cleavage of their corresponding N-acetyl-DL-derivatives

Acylase I from Aspergillus oryzae is an even more useful enzyme than suggested so far. Besides standard amino acids such as L-Met, L-Val and L-Phe, a number of additional sulfur- and selenium-containing amino acids can be obtained at useful reaction rates and in very high enantiomeric purity by kinetic resolution of the respective N-acetyl-DL-amino acids.

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

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.

ENANTIOSELECTIVE HYDROLYSIS BY BAKER'S YEAST

Optically active N-acetylamino acid esters were obtained by enantioselective hydrolysis of their racemates using fermenting baker's yeast.