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Related Experiment Videos

Aminoglycoside-modifying enzymes.

G D Wright1

  • 1Antimicrobial Research Centre Department of Biochemistry McMaster University 1200 Main Street West, Hamilton, ON L8N 3Z5, Canada. wrightge@fhs.mcmaster.ca.

Current Opinion in Microbiology
|October 6, 1999
PubMed
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Bacterial resistance to aminoglycoside antibiotics often stems from modifying enzymes. Crystal structures and genome data reveal new insights into these resistance mechanisms and related enzyme families.

Area of Science:

  • Microbiology
  • Structural Biology
  • Genomics

Background:

  • Bacterial resistance to aminoglycoside antibiotics is a significant clinical challenge.
  • This resistance is primarily mediated by enzymatic modification of the antibiotics.
  • Key modifying enzymes include phosphotransferases, nucleotidyltransferases, and acetyltransferases.

Purpose of the Study:

  • To review the current understanding of aminoglycoside-modifying enzymes.
  • To highlight insights gained from recent crystal structure determinations.
  • To explore connections between these enzymes and other enzyme families, and identify potential resistance elements from genomic data.

Main Methods:

  • Analysis of published crystal structures of aminoglycoside-modifying enzymes.

Related Experiment Videos

  • Review of bacterial genome sequences to identify potential resistance genes.
  • Comparative analysis of enzyme structures and functions.
  • Main Results:

    • Crystal structures for all three major classes of aminoglycoside-modifying enzymes are now available.
    • These structures reveal unexpected functional and evolutionary links to other enzyme families.
    • Genomic analysis has identified numerous potential aminoglycoside resistance determinants in various bacteria.

    Conclusions:

    • Structural biology has significantly advanced the understanding of aminoglycoside resistance mechanisms.
    • Emerging connections between modifying enzymes and other enzyme families offer new avenues for research.
    • Genomic data provides a comprehensive view of the prevalence of aminoglycoside resistance elements.