155264-06-5

Upstream product

• 86030-43-5 N,N-diisopropylmethylphosphonamidic chloride 
• 39947-04-1 N-6-benzoyl-2',3'-O-isopropylideneadenosine 

Downstream Products

• 256642-99-6 Carbonic acid 4-((S)-3-{[(3aR,4R,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethoxy]-methoxy-phosphoryloxy}-2-benzyloxycarbonylamino-propyl)-phenyl ester benzyl ester 
• 256643-00-2 Phosphoric acid (S)-2-amino-3-(4-hydroxy-phenyl)-propyl ester (3aR,4R,6R,6aR)-6-(6-amino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethyl ester 
• 6372-08-3 Phosphoric acid (S)-2-amino-3-(4-hydroxy-phenyl)-propyl ester (2R,3S,4R,5R)-5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl ester 

Relevant academic research and scientific papers

Improved synthesis of biotinol-5′-AMP: Implications for antibacterial discovery

An improved synthesis of biotinol-5′-AMP, an acyl-AMP mimic of the natural reaction intermediate of biotin protein ligase (BPL), is reported. This compound was shown to be a pan inhibitor of BPLs from a series of clinically important bacteria, particularl

Molecular recognition of tyrosinyl adenylate analogues by prokaryotic tyrosyl tRNA synthetases

Molecular modelling and synthetic studies have been carried out on tyrosinyl adenylate and analogues to probe the interactions seen in the active site of the X-ray crystal structure of tyrosyl tRNA synthetase from Bacillus stearothermophilus, and to search for new inhibitors of this enzyme. Micromolar and sub-micromolar inhibitors of tyrosyl tRNA synthetases from both B. stearothermophilus and Staphylococcus aureus have been synthesised. The importance of the adenine ring to the binding of tyrosinyl adenylate to the enzyme, and the importance of water-mediated hydrogen bonding interactions, have been highlighted. The inhibition data has been further supported by homology modelling with the S. aureus enzyme, and by ligand docking studies. (C) 1999 Elsevier Science Ltd.

Glutamyl adenylate analogues are inhibitors of glutamyl-tRNA synthetase

Glutamol adenylate 10 was a competitive inhibitor (K(i) = 3 μM) of glutamyl-tRNA synthetase from Escherichia coli. The N6-benzoyl adenine derivative 9 was also an inhibitor (K(i) ~ 60 μM). Replacement of adenine by other bases (purine, cytosine