1263056-98-9

Basic information

• Product Name: C₂₇H₄₈N₇O₁₈P
• CAS NO: 1263056-98-9
• Molecular Weight: 789.688
• Mol File: 1263056-98-9.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: C₂₇H₄₈N₇O₁₈P(CAS DataBase Reference)
• NIST Chemistry Reference: C₂₇H₄₈N₇O₁₈P(1263056-98-9)
• EPA Substance Registry System: C₂₇H₄₈N₇O₁₈P(1263056-98-9)

Safety Data

• Hazardous Substances Data: 1263056-98-9(Hazardous Substances Data)

Upstream product

• 63-37-6 cytidine monophosphate 
• 59-01-8 kanamycin A 

Relevant articles and documents

Dissecting the cosubstrate structure requirements of the Staphylococcus aureus aminoglycoside resistance enzyme ANT(4′)

Aminoglycosides are important antibiotics used against a wide range of pathogens. As a mechanism of defense, bacteria have evolved enzymes able to inactivate these drugs by regio-selectively adding a variety of functionalities (acetyl, phospho, and nucelotidyl groups) to their scaffolds. The aminoglycoside nucleotidyltransferase ANT(4′) is one of the most prevalent and unique modifying-enzymes. Here, by TLC, HRMS, and colorimetric assays, we demonstrate that the resistance enzyme ANT(4′) from Staphylococcus aureus is highly substrate and cosubstrate promiscuous. We show that deoxy-ribonucleotide triphosphates (dNTPs) are better cosubstrates than NTPs. We demonstrate that the position of the triphosphate group (5′ and not 3′) on the ribose/deoxyribose ring is important for recognition by ANT(4′), and that NTPs with larger substituents at the 3′-position of the ribose ring are not cosubstrates for ANT(4′). We confirm that for all aminoglycosides tested, the respective nucleotidylated products are completely inactive. These results provide valuable insights into the development of strategies to combat the ever-growing bacterial resistance problem.