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Dissecting the cosubstrate structure requirements of the Staphylococcus aureus aminoglycoside resistance enzyme ANT(4').

Abstract：

:Aminoglycosides are important antibiotics used against a wide range of pathogens. As a mechanism of defense, bacteria have evolved enzymes able to inactivate these drugs by regio-selectively adding a variety of functionalities (acetyl, phospho, and nucelotidyl groups) to their scaffolds. The aminoglycoside nucleotidyltransferase ANT(4') is one of the most prevalent and unique modifying-enzymes. Here, by TLC, HRMS, and colorimetric assays, we demonstrate that the resistance enzyme ANT(4') from Staphylococcus aureus is highly substrate and cosubstrate promiscuous. We show that deoxy-ribonucleotide triphosphates (dNTPs) are better cosubstrates than NTPs. We demonstrate that the position of the triphosphate group (5' and not 3') on the ribose/deoxyribose ring is important for recognition by ANT(4'), and that NTPs with larger substituents at the 3'-position of the ribose ring are not cosubstrates for ANT(4'). We confirm that for all aminoglycosides tested, the respective nucleotidylated products are completely inactive. These results provide valuable insights into the development of strategies to combat the ever-growing bacterial resistance problem.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Porter VR,Green KD,Zolova OE,Houghton JL,Garneau-Tsodikova S

doi

10.1016/j.bbrc.2010.10.119

subject

Has Abstract

pub_date

2010-12-03 00:00:00

pages

85-90

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)02008-5

journal_volume

403

pub_type

杂志文章

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