title: Aminoglycoside-modifying enzymes.
abstract: Bacterial resistance to the aminoglycoside antibiotics is most frequently associated with the expression of modifying enzymes that can phosphorylate, adenylate or acetylate these compounds. The recent availability of representative crystal structures for all three classes of modifying enzymes has greatly expanded our knowledge of enzyme function, and has revealed unexpected and exciting connections to other families of enzymes. Furthermore, the complete genome sequences for several bacteria have revealed many potential aminoglycoside-resistance elements.
authors.affiliation: Antimicrobial Research Centre Department of Biochemistry McMaster University 1200 Main Street West, Hamilton, ON L8N 3Z5, Canada. wrightge@fhs.mcmaster.ca.
authors.forename: G D
authors.initials: GD
authors.lastname: Wright
mesh_terms: D000123:Acetyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D000617:Aminoglycosides; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D004352:Drug Resistance, Microbial; D004791:Enzyme Inhibitors / Q000494:pharmacology; D051379:Mice; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D004791:Enzyme Inhibitors; D000123:Acetyltransferases; C019681:aminoglycoside acetyltransferase; D017853:Phosphotransferases (Alcohol Group Acceptor); D009713:Nucleotidyltransferases