17029-36-6Relevant academic research and scientific papers
Nucleoside triphosphate cosubstrates control the substrate profile and efficiency of aminoglycoside 3′-O-phosphotransferase type IIa
Holbrook, Selina Y. L.,Gentry, Matthew S.,Tsodikov, Oleg V.,Garneau-Tsodikova, Sylvie
, p. 1332 - 1339 (2018)
Aminoglycosides (AGs) are broad-spectrum antibiotics that play an important role in the control and treatment of bacterial infections. Despite the great antibacterial potency of AGs, resistance to these antibiotics has limited their clinical applications. The AG 3′-O-phosphotransferase of type IIa (APH(3′)-IIa) encoded by the neoR gene is a common bacterial AG resistance enzyme that inactivates AG antibiotics. This enzyme is used as a selection marker in molecular biology research. APH(3′)-IIa catalyzes the transfer of the γ-phosphoryl group of ATP to an AG at its 3′-OH group. Although APH(3′)-IIa has been reported to utilize exclusively ATP as a cosubstrate, we demonstrate that this enzyme can utilize a broad array of NTPs. By substrate profiling, TLC, and enzyme kinetics experiments, we probe AG phosphorylation by APH(3′)-IIa with an extensive panel of substrates and cosubstrates (13 AGs and 10 NTPs) for the purpose of gaining a thorough understanding of this resistance enzyme. We find, for the first time, that the identity of the NTP cosubstrate dictates the set of AGs modified by APH(3′)-IIa and the phosphorylation efficiency for different AGs.
Mass Spectral and 13C N.M.R. Analyses of Aminoglycoside Aminocyclitols Modified by Enzyme-Catalysed Reactions
Coombe, Reginald G.,George, Anthony M.
, p. 547 - 554 (2007/10/02)
Chemical and physical analytical methods, including mass spectrometry and 13C n.m.r., have been applied to the evaluation of the structures of the inactivated products of enzyme-mediated transferase reactions.Evidence is presented for the assignment of st
