7743-39-7

Usage

Uses

Used in Pharmaceutical Industry:
3,5-bis(acetylamino)benzoic acid is used as a key intermediate for the synthesis of various pharmaceuticals and organic compounds. Its unique structure and properties make it an essential component in the development of new drugs and therapeutic agents.
Used in Biochemistry Research:
3,5-bis(acetylamino)benzoic acid is used as a valuable tool for studying carbohydrate-protein interactions. Its role in understanding these interactions is crucial for advancing our knowledge of biological processes and the development of targeted therapies.
Used in Organic Synthesis:
3,5-bis(acetylamino)benzoic acid is used as a building block for the synthesis of complex organic molecules. Its versatility and reactivity make it an important component in the creation of a wide range of organic compounds.
Used in Connective Tissue Formation:
As a key component of glycosaminoglycans, 3,5-bis(acetylamino)benzoic acid plays a vital role in the formation of connective tissues in the human body. Its contribution to the structural integrity and function of these tissues is essential for maintaining overall health and well-being.

InChI:InChI=1/C11H12N2O4/c1-6(14)12-9-3-8(11(16)17)4-10(5-9)13-7(2)15/h3-5H,1-2H3,(H,12,14)(H,13,15)(H,16,17)/p-1

Upstream product

• 535-87-5 3.5-diaminobenzoic acid 
• 75-36-5 acetyl chloride 
• 108-24-7 acetic anhydride 

Downstream Products

• 1713-07-1 2,4,6,triiodo-5-amino-3-acetylaminobenzoic acid 
• 139870-31-8 meso-mono<α-o-(3,5-diacetamidobenzenecarboxamido)phenyl>tris(α,α,α-o-pivalamidophenyl)porphyrin 

Relevant academic research and scientific papers

Water soluble lanthanoid benzoate complexes for the kinetic separation of cis/trans-limonene oxide

A new class of water soluble, environmentally friendly, lanthanoid 3,5-diacetamidobenzoate complexes (Ln = La, Gd, Yb) have been synthesized. The La and Gd complexes selectively catalyse hydrolysis of the cis-isomer of limonene oxide allowing for the separation of the trans-isomer (>98:2 dr) in up to 74% yield. Comparative studies with the corresponding chlorides and triflates reveal the lanthanoid benzoate complexes to be more active than the chlorides, but less active, though more selective, than the triflates.

O2 and CO Binding Behavior of Double-Sided Porphyrinatoiron(II) Complexes Modified by Amide Residues

New double-sided porphyrinatoiron(II) complexes having a polar cavity which includes an amide moiety (5,10,15-tris-20--6-(3,3-dimethylbutyryloxy)phenyl>porphinatoiron(II) (1b) and 5,10,15-tris-20--6-(3,3-dimethylbutyryloxy)phenyl>porphinatoiron(II) (2b)) were synthesized. 1H NMR spectroscopy indicated that the amide residues are located on the porphyrin ring plane.The O2 and CO binding affinities of 1b and 2b were higher than those of 5,10,15,20-tetrakisporphinatoiron(II) (4b), in response to the local polarity in the cavity.The polar amide residue resulted in a decreased O2 dissociation rate.Thermodynamic parameters for the gaseous ligand bindings to the 2b complex were also determined.

H-bonded oxyhemoglobin models with substituted picket-fence porphyrins: The model compound equivalent of site-directed mutagenesis

Iron(II) complexes of picket-fence-type porphyrins having one of the four pivalamide pickets replaced by a substituent capable of H-bonding have been synthesized as models for oxyhemoglobin. This synthetic approach is analogous to site-directed mutagenesis of the distal residues in oxygen-binding hemoproteins. Rate and equilibrium data for dioxygen binding have been determined to evaluate the effect of the H-bonding substituent and to make comparisons with more passive substituents. The effect of H-bonding on the dioxygen affinity under standard conditions (25 °C, toluene solvent, 1,2-dimethylimidazole as axial ligand) is best illustrated by the ca. 10-fold increase observed when one pivalamide substituent of picket-fence porphyrin is replaced by a phenylurea substituent. Other substituents influence dioxygen adduct stability in a variety of ways to reveal that even with an apparently straightforward systematic approach, there can be considerable difficulty in partitioning the various factors that influence O2 affinity. This applies to both model compounds and mutant proteins.