913094-93-6

Upstream product

• 92762-93-1 β-benzyl L-isoasparaginate 
• 541-88-8 Chloroacetic anhydride 
• 2177-63-1 (S)-2-amino-4-(benzyloxy)-4-oxobutanoic acid 
• 87421-27-0 N-t-butyloxycarbonyl-L-aspartic acid β-benzyl ester α-amide 
• 7536-58-5 BOC-L-aspartic acid 4-benzyl ester 

Downstream Products

• 913094-94-7 β-benzyl N-(diethoxyphosphinoyl)acetyl-L-isoasparaginate 
• 913094-95-8 β-benzyl N-phosphonoacetyl-L-isoasparaginate 

Relevant academic research and scientific papers

N-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase

The synthesis of a new inhibitor, N-phosphonacetyl-L-isoasparagine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as structural studies of the enzyme·PALI complex. PALI was synthesized in 7 steps from β-benzyl L-aspartate. The KD of PALI was 2 μM. Kinetics and small-angle X-ray scattering experiments showed that PALI can induce the cooperative transition of ATCase from the T to the R state. The X-ray structure of the enzyme·PALI complex showed 22 hydrogen-bonding interactions between the enzyme and PALI. The kinetic characterization and crystal structure of the ATCase·PALI complex also provides detailed information regarding the importance of the α-carboxylate for the binding of the substrate aspartate.