The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

aac(3)-I  -  aminoglycoside acetyltransferase

Pseudomonas aeruginosa

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of aac(3)-I


High impact information on aac(3)-I

  • The variable region of the integron also contained a bla(VIM-1) metallo-beta-lactamase cassette and a duplicated aacA4 aminoglycoside acetyltransferase cassette [3].
  • These isolates had a delayed development of a red pigment and exhibited a similar antibiotype (resistance to all beta-lactams except for imipenem and to gentamicin, tobramycin, netilmicin, ciprofloxacin, and rifampin) associated with the production of the TEM-21 beta-lactamase and a type II 3'-N-aminoglycoside acetyltransferase [AAC(3)-II] enzyme [4].
  • It was found to code for two gentamicin modifying enzymes, which from their substrate profile by radioenzymatic assay were characterized as aminoglycoside acetyltransferase AAC(3)-I and aminoglycoside adenylyltransferase AAD(2") [5].

Chemical compound and disease context of aac(3)-I


Biological context of aac(3)-I

  • Homology between the flanking sequences of both aac(3)-I genes and other resistance determinants known to reside in integron environments was also observed [2].

Associations of aac(3)-I with chemical compounds


  1. Multidrug-resistant Pseudomonas aeruginosa strain that caused an outbreak in a neurosurgery ward and its aac(6')-Iae gene cassette encoding a novel aminoglycoside acetyltransferase. Sekiguchi, J., Asagi, T., Miyoshi-Akiyama, T., Fujino, T., Kobayashi, I., Morita, K., Kikuchi, Y., Kuratsuji, T., Kirikae, T. Antimicrob. Agents Chemother. (2005) [Pubmed]
  2. Cloning and characterization of a 3-N-aminoglycoside acetyltransferase gene, aac(3)-Ib, from Pseudomonas aeruginosa. Schwocho, L.R., Schaffner, C.P., Miller, G.H., Hare, R.S., Shaw, K.J. Antimicrob. Agents Chemother. (1995) [Pubmed]
  3. OXA-46, a new class D beta-lactamase of narrow substrate specificity encoded by a blaVIM-1-containing integron from a Pseudomonas aeruginosa clinical isolate. Giuliani, F., Docquier, J.D., Riccio, M.L., Pagani, L., Rossolini, G.M. Antimicrob. Agents Chemother. (2005) [Pubmed]
  4. Prolonged outbreak of infection due to TEM-21-producing strains of Pseudomonas aeruginosa and enterobacteria in a nursing home. Dubois, V., Arpin, C., Noury, P., Andre, C., Coulange, L., Quentin, C. J. Clin. Microbiol. (2005) [Pubmed]
  5. Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa. Angelatou, F., Litsas, S.B., Kontomichalou, P. J. Antibiot. (1982) [Pubmed]
  6. Integron-located oxa-32 gene cassette encoding an extended-spectrum variant of OXA-2 beta-lactamase from Pseudomonas aeruginosa. Poirel, L., Gerome, P., De Champs, C., Stephanazzi, J., Naas, T., Nordmann, P. Antimicrob. Agents Chemother. (2002) [Pubmed]
  7. Plasmid-mediated high-level gentamicin resistance among enteric bacteria isolated from pet turtles in Louisiana. Díaz, M.A., Cooper, R.K., Cloeckaert, A., Siebeling, R.J. Appl. Environ. Microbiol. (2006) [Pubmed]
WikiGenes - Universities