Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
Article Abstract:
Resistance of bacteria to aminoglycoside antibiotics can be attributed to antibacterial agent such as phosphorylation, adenylylation and acetylation. Aminoglycoside antibiotics comes from the breaking down of phosphorylation through the catalytic action of aminoglycoside kinase, APH(3')-IIIa. Although an observable complete lack of of sequence homology, the three-dimensional fold of APH(3')-IIIa shows noticeable likeness to eukaryotic protein kinases. Thus, it is considered that a common ancestor is shared by APH(3') enzymes and eukaryotic-type protein kinases based on the research results.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
Article Abstract:
The genetic mechanisms and evolution and relatedness of aminoglycoside resistance enzymes are presented. Studies have revealed the presence of genetically encoded aminoglycoside-modifying enzymes which inactivate the anti-bacterial agent and had shown that aminoglycoside resistance may be acquired from other resistant organisms or as a result of genetic alteration. The genetic spread has been found to be induced by various genetic elements such as plasmids, integrons and transposons.
Publication Name: Microbiological Reviews
Subject: Biological sciences
ISSN: 0146-0749
Year: 1993
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Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
Article Abstract:
The extracellular solute-binding bacteria function as receptors in chemoreception and transmembrane transportation. Interaction of transmembrane chemoreception takes place when there are solute-binding changes in the periplasmic binding proteins of gram-negative bacteria. The majority of the proteins can be grouped into eight families with regard to their specificity. The solute-binding proteins also help in signal transduction.
Publication Name: Microbiological Reviews
Subject: Biological sciences
ISSN: 0146-0749
Year: 1993
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