Gentamicin 2"-nucleotidyltransferase

From WikiMD's Wellness Encyclopedia

Gentamicin 2"-nucleotidyltransferase is an enzyme that in humans is encoded by the AAC(2') gene. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is adenylyltransferase.

Function[edit | edit source]

Gentamicin 2"-nucleotidyltransferase is an aminoglycoside modifying enzyme that confers resistance to aminoglycoside antibiotics in many Gram-negative bacteria. It does this by catalyzing the transfer of the adenylyl group from ATP to the 2"-hydroxyl of the aminoglycoside substrate.

Structure[edit | edit source]

The enzyme is a monomer with a molecular weight of approximately 30 kDa. It contains a single active site that binds both the aminoglycoside and ATP substrates. The active site is located in a deep cleft between two domains of the enzyme, and is accessible through a narrow channel.

Clinical significance[edit | edit source]

Resistance to aminoglycoside antibiotics is a significant problem in the treatment of bacterial infections. Understanding the structure and function of aminoglycoside modifying enzymes like gentamicin 2"-nucleotidyltransferase is important for the development of new antibiotics that can overcome this resistance.

See also[edit | edit source]

References[edit | edit source]


WikiMD
Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD

Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD

WikiMD's Wellness Encyclopedia

Let Food Be Thy Medicine
Medicine Thy Food - Hippocrates

WikiMD is not a substitute for professional medical advice. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.

Contributors: Prab R. Tumpati, MD