26117-27-1

Basic information

• Product Name: Nalpha-Acetyl-D-asparagine
• Synonyms: N-ACETYL-D-ASPARAGINE;N-ALPHA-ACETYL-D-ASPARAGINE;n2-acetyl-d-asparagine;ACETYL-D-ASPARAGINE;AC-D-ASN-OH;AC-D-ASPARAGINE;2-(acetylamino)-4-amino-4-oxobutanoic acid;na-acetyl-D-asparagine
• CAS NO: 26117-27-1
• Molecular Formula: C₆H₁₀N₂O₄
• Molecular Weight: 174.15
• EINECS: 247-468-4
• Product Categories: A - H;Amino Acids;Modified Amino Acids
• Mol File: 26117-27-1.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 588.7 °C at 760 mmHg
• Flash Point: 309.8 °C
• Appearance: /
• Density: 1.346 g/cm³
• Vapor Pressure: 2.2E-15mmHg at 25°C
• Refractive Index: 1.508
• Storage Temp.: 2-8°C
• PKA: 3.45±0.10(Predicted)
• CAS DataBase Reference: Nalpha-Acetyl-D-asparagine(CAS DataBase Reference)
• NIST Chemistry Reference: Nalpha-Acetyl-D-asparagine(26117-27-1)
• EPA Substance Registry System: Nalpha-Acetyl-D-asparagine(26117-27-1)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 26117-27-1(Hazardous Substances Data)

Usage

Description

Nalpha-Acetyl-D-asparagine is a synthetic derivative of D-asparagine, an amino acid naturally occurring in certain plant and animal proteins. As a chemical compound, it is known for its enhanced stability and solubility due to its acetylated form, making it a valuable tool in the synthesis of novel peptides and proteins. Its unique properties and versatility contribute to its potential applications in pharmaceuticals, biotechnology, and the study of peptide and protein structure-function relationships.

Uses

Used in Pharmaceutical Development:
Nalpha-Acetyl-D-asparagine is used as a building block in the synthesis of novel peptides and proteins for pharmaceutical applications. Its enhanced stability and solubility contribute to the development of more effective and stable drug candidates.
Used in Biochemistry Research:
In the field of biochemistry, Nalpha-Acetyl-D-asparagine is used as a valuable tool for studying the structure-function relationships of peptides and proteins. Its unique properties allow researchers to gain insights into the fundamental mechanisms of these biomolecules.
Used in Biotechnology Products:
Nalpha-Acetyl-D-asparagine may have potential applications in the development of biotechnology products, such as engineered proteins with specific functions or improved properties. Its versatility and chemical stability make it a promising candidate for various biotechnological applications.
Used in Drug Discovery:
In the realm of drug discovery, Nalpha-Acetyl-D-asparagine serves as a valuable chemical for the design and synthesis of new drug candidates. Its unique properties can contribute to the development of innovative therapeutic agents with improved efficacy and safety profiles.

InChI:InChI=1/C6H10N2O4/c1-3(9)8-4(6(11)12)2-5(7)10/h4H,2H2,1H3,(H2,7,10)(H,8,9)(H,11,12)/t4-/m1/s1

Upstream product

• 14464-29-0 N-acetoxysuccinimide 
• 4474-86-6 (R)-4-amino-2-(((benzyloxy)carbonyl)amino)-4-oxobutanoic acid 
• 16473-76-0 N-acetylasaparagine 

Relevant articles and documents

In Vitro Characterization of the Colibactin-Activating Peptidase ClbP Enables Development of a Fluorogenic Activity Probe

The gut bacterial genotoxin colibactin is linked to the development of colorectal cancer. In the final stages of colibactin's biosynthesis, an inactive precursor (precolibactin) undergoes proteolytic cleavage by ClbP, an unusual inner-membrane-bound periplasmic peptidase, to generate the active genotoxin. This enzyme presents an opportunity to monitor and modulate colibactin biosynthesis, but its active form has not been studied in vitro and limited tools exist to measure its activity. Here, we describe the in vitro biochemical characterization of catalytically active, full-length ClbP. We elucidate its substrate preferences and use this information to develop a fluorogenic activity probe. This tool will enable the discovery of ClbP inhibitors and streamline identification of colibactin-producing bacteria.

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.