117821-34-8

Basic information

• Product Name: 4-[(2-HYDROXYETHYL)AMINO]BENZOIC ACID
• Synonyms: 4-[(2-HYDROXYETHYL)AMINO]BENZOIC ACID
• CAS NO: 117821-34-8
• Molecular Formula: C₉H₁₁NO₃
• Molecular Weight: 181.19
• Mol File: 117821-34-8.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 4-[(2-HYDROXYETHYL)AMINO]BENZOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 4-[(2-HYDROXYETHYL)AMINO]BENZOIC ACID(117821-34-8)
• EPA Substance Registry System: 4-[(2-HYDROXYETHYL)AMINO]BENZOIC ACID(117821-34-8)

Safety Data

• Hazardous Substances Data: 117821-34-8(Hazardous Substances Data)

Upstream product

• 75-21-8 oxirane 
• 150-13-0 4-amino-benzoic acid 
• 141-46-8 Glycolaldehyde 
• 126993-07-5 methyl 4-[N-(2-hydroxyethyl)amino]benzoate 
• 619-45-4 4-methoxycarbonyl aniline 
• 855199-07-4 4-(2-methoxy-ethylamino)-benzoic acid 

Downstream Products

• 122-98-5 2-Anilinoethanol 
• 15719-64-9 methylammonium carbonate 

Relevant articles and documents

Glycolaldehyde is an endogenous source of lysine N-pyrrolation

Lysine N-pyrrolation converts lysine residues to Nα-pyrrole-L-lysine (pyrK) in a covalent modification reaction that significantly affects the chemical properties of proteins, causing them to mimic DNA. pyrK in proteins has been detected in vivo, indicating that pyrrolation occurs as an endogenous reaction. However, the source of pyrK remains unknown. In this study, on the basis of our observation in vitro that pyrK is present in oxidized low-density lipoprotein and in modified proteins with oxidized polyunsaturated fatty acids, we used LC– electrospray ionization–MS/MS coupled with a stable isotope dilution method to perform activity-guided separation of active molecules in oxidized lipids and identified glycolaldehyde (GA) as a pyrK source. The results from mechanistic experiments to study GA-mediated lysine N-pyrrolation suggested that the reactions might include GA oxidation, generating the dialdehyde glyoxal, followed by condensation reactions of lysine amino groups with GA and glyoxal. We also studied the functional significance of GA-mediated lysine N-pyrrolation in proteins and found that GA-modified proteins are recognized by apolipoprotein E, a binding target of pyrrolated proteins. Moreover, GA-modified proteins triggered an immune response to pyrrolated proteins, and monoclonal antibodies generated from mice immunized with GA-modified proteins specifically recognized pyrrolated proteins. These findings reveal that GA is an endogenous source of DNA-mimicking pyrrolated proteins and may provide mechanistic insights relevant for innate and autoimmune responses associated with glucose metabolism and oxidative stress.