Domain dissection and characterization of the aminoglycoside resistance enzyme ANT(3″)-Ii/AAC(6')-IId from Serratia marcescens.

ABSTRACT: Aminoglycosides (AGs) are broad-spectrum antibiotics whose constant use and presence in growth environments has led bacteria to develop resistance mechanisms to aid in their survival. A common mechanism of resistance to AGs is their chemical modification (nucleotidylation, phosphorylation, or acetylation) by AG-modifying enzymes (AMEs). Through evolution, fusion of two AME-encoding genes has resulted in bifunctional enzymes with broader spectrum of activity. Serratia marcescens, a human enteropathogen, contains such a bifunctional enzyme, ANT(3″)-Ii/AAC(6')-IId. To gain insight into the role, effect, and importance of the union of ANT(3″)-Ii and AAC(6')-IId in this bifunctional enzyme, we separated the two domains and compared their activity to that of the full-length enzyme. We performed

SUBMITTER: Green KD 

PROVIDER: S-EPMC3646955 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature