106873-99-8

Basic information

• Product Name: 2-N-FORMYLAMIONO-BUTYRICACID
• Synonyms: 2-N-FORMYLAMIONO-BUTYRICACID;2-N-Formyl amino-butyric acid;Butanoic acid, 2-(forMylaMino)-;N-FORMYL-L-2-AMINOBUTYRIC ACID;N-Formyl-DL-2-aminobutyric Acid
• CAS NO: 106873-99-8
• Molecular Formula: C₅H₉NO₃
• Molecular Weight: 131.13
• Mol File: 106873-99-8.mol
• Article Data: 1

Chemical Properties

• Melting Point: 153.0 to 157.0 °C
• Boiling Point: 242.42°C (rough estimate)
• Appearance: /
• Density: 1.3121 (rough estimate)
• Refractive Index: 1.4300 (estimate)
• Storage Temp.: 2-8°C
• Water Solubility: 33.57g/L(25 oC)
• CAS DataBase Reference: 2-N-FORMYLAMIONO-BUTYRICACID(CAS DataBase Reference)
• NIST Chemistry Reference: 2-N-FORMYLAMIONO-BUTYRICACID(106873-99-8)
• EPA Substance Registry System: 2-N-FORMYLAMIONO-BUTYRICACID(106873-99-8)

Safety Data

• Hazardous Substances Data: 106873-99-8(Hazardous Substances Data)

Usage

General Description

2-N-Formylamino-butyric acid is a chemical compound characterized by the presence of a formylamino functional group attached to a butyric acid molecule. The functionality of this compound is often found in degradable polymers, food packaging, drug delivery systems, biosensors, and coating materials. Its structure consists of both hydrophilic and hydrophobic parts, meaning it is both soluble in water and in oils, fats, and organic solvents. Owing to its structural properties, this compound can also act as a buffer to balance or stabilize pH within a substance or solution. Precise data and details about its toxicity or safety are not readily available, suggesting there is still ongoing study about this compound. Therefore, proper caution and safety mechanisms should be employed in its use and handling.

Upstream product

• 64-18-6 formic acid 
• 2835-81-6 2-aminobutanoic acid 

Downstream Products

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

Relevant articles and documents

Remote binding energy in antibody catalysis: Studies of a catalytically unoptimized specificity pocket

Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system. We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes. We have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes favorable simultaneous interactions between the side chain and binding pocket along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-pocket interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (kcat) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8·hapten complex has allowed for the identification of differences between the active sites of 17E8 and several proteases. The identified differences give insight to the sources of the inefficient use of binding energy.