The use of neamine as a molecular template: Inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3′-phosphotransferase type IIa

Bioorganic & Medicinal Chemistry Letters
1998.0

Abstract

Aminoglycoside 3'-phosphotransferase type IIa [APH(3')-IIa] is a member of the family of bacterial aminoglycoside-modifying enzymes. Bacteria that harbor these enzymes are resistant to aminoglycoside antibiotics. Four aminoglycoside-based affinity inactivators were synthesized and were shown to be both substrates and inactivators for APH(3')-IIa. These affinity inactivators are N-bromoacetylated derivatives of neamine, an aminoglycoside antibiotic, where the bromoacetyl moiety in each was introduced regiospecifically at a different amine of the parent compound.

Knowledge Graph

Similar Paper

The use of neamine as a molecular template: Inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3′-phosphotransferase type IIa
Bioorganic & Medicinal Chemistry Letters 1998.0
New Broad-Spectrum Antibacterial Amphiphilic Aminoglycosides Active against Resistant Bacteria: From Neamine Derivatives to Smaller Neosamine Analogues
Journal of Medicinal Chemistry 2016.0
Synthesis and Antimicrobial Evaluation of Amphiphilic Neamine Derivatives
Journal of Medicinal Chemistry 2010.0
Synthesis of (+),(−)-neamine and their positional isomers as potential antibiotics
Bioorganic & Medicinal Chemistry Letters 2003.0
Aminoglycoside antibiotics. 3. Epimino derivatives of neamine, ribostamycin, and kanamycin B
Journal of Medicinal Chemistry 1980.0
Overexpression and Initial Characterization of the Chromosomal Aminoglycoside 3′- O -Phosphotransferase APH(3′)-IIb from Pseudomonas aeruginosa
Antimicrobial Agents and Chemotherapy 2007.0
Aph(3′)-IIc, an Aminoglycoside Resistance Determinant from Stenotrophomonas maltophilia
Antimicrobial Agents and Chemotherapy 2007.0
Broad-spectrum antibacterial amphiphilic aminoglycosides: A new focus on the structure of the lipophilic groups extends the series of active dialkyl neamines
European Journal of Medicinal Chemistry 2018.0
Mutant APH(2″)-IIa Enzymes with Increased Activity against Amikacin and Isepamicin
Antimicrobial Agents and Chemotherapy 2010.0
Synthesis and antibacterial activity of novel neamine derivatives
Bioorganic & Medicinal Chemistry Letters 2006.0