Skip to main content

Gentamicin 3′-N-acetyltransferase

  • Chapter
Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 30))

  • 87 Accesses

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Williams, J.W.; Northrop, D.B.: Purification and properties of gentamicin acetyltransferase I. Biochemistry, 15, 125–131 (1976)

    Article  PubMed  CAS  Google Scholar 

  2. Biddlecome, S.; Haas, M.; Davies, J.; Rane, D.F.; Daniels, P.J.L.: Enzymatic modification of aminoglycoside antibiotics: a new 3-N-acetylating enzyme from a Pseudomonas aeruginosa isolate. Antimicrob. Agents Chemother., 9, 951–955 (1976)

    PubMed  CAS  Google Scholar 

  3. Angelatou, R; Litsas, S.B.; Kontomichalou, P.: Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa. J. Antibiot., 35, 235–244 (1982)

    PubMed  CAS  Google Scholar 

  4. Williams, J.W.; Northrop, D.B.: Kinetic mechanisms of gentamicin acetyltransferase I. Antibiotic-dependent shift from rapid to nonrapid equilibrium random mechanisms. J. Biol. Chem., 253, 5902–5907 (1978)

    PubMed  CAS  Google Scholar 

  5. Williams, J.W.; Northrop, D.B.: Substrate specificity and structure-activity relationships of gentamicin acetyltransferase I. The dependence of antibiotic resistance upon substrate Vmax/Km values. J. Biol. Chem., 253, 5908–5914 (1978)

    PubMed  CAS  Google Scholar 

  6. Vliegenthart, John S.; Ketelaar-Van Gaalen, Petra A. G.; Van de Klundert, Jos A. M.: Identification of three genes coding for aminoglycoside-modifying enzymes by means of the polymerase chain reaction. J. Antimicrob. Chemother., 25, 759–765 (1990)

    Article  PubMed  CAS  Google Scholar 

  7. Bongaerts, Ger P. A.; Vliegenthart, John S.: Effect of aminoglycoside concentration on reaction rates of aminoglycoside-modifying enzymes. Antimicrob. Agents Chemother., 32, 740–746 (1988)

    PubMed  CAS  Google Scholar 

  8. Gomez-Lus, R.; Gomez-Lus, S.; Goni, M. P.; Rivera, M. J.; Martin, C; Rubio-Calvo, M. C: Stability of dactimicin to aminoglycoside-modifying enzymes produced by 341 bacterial clinical isolates. Drugs Exp. Clin. Res., 15, 129–132 (1989)

    PubMed  CAS  Google Scholar 

Download references

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2006 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

(2006). Gentamicin 3′-N-acetyltransferase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 30. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37717-4_1

Download citation

Publish with us

Policies and ethics