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1.
Curr Protein Pept Sci ; 25(6): 454-468, 2024.
Article in English | MEDLINE | ID: mdl-38314602

ABSTRACT

A comprehensive knowledge of aminoglycoside-modifying enzymes (AMEs) and their role in bacterial resistance mechanisms is urgently required due to the rising incidence of antibiotic resistance, particularly in Klebsiella pneumoniae infections. This study explores the essential features of AMEs, including their structural and functional properties, the processes by which they contribute to antibiotic resistance, and the therapeutic importance of aminoglycosides. The study primarily examines the Recombinant Klebsiella pneumoniae Aminoglycoside Adenylyl Transferase (RKAAT), particularly emphasizing its biophysical characteristics and the sorts of resistance it imparts. Furthermore, this study examines the challenges presented by RKAAT-mediated resistance, an evaluation of treatment methods and constraints, and options for controlling infection. The analysis provides a prospective outlook on strategies to address and reduce antibiotic resistance. This extensive investigation seeks to provide vital insights into the continuing fight against bacterial resistance, directing future research efforts and medicinal approaches.


Subject(s)
Aminoglycosides , Anti-Bacterial Agents , Klebsiella pneumoniae , Klebsiella pneumoniae/drug effects , Klebsiella pneumoniae/genetics , Aminoglycosides/pharmacology , Aminoglycosides/chemistry , Anti-Bacterial Agents/pharmacology , Anti-Bacterial Agents/chemistry , Humans , Drug Resistance, Bacterial/drug effects , Bacterial Proteins/metabolism , Bacterial Proteins/genetics , Bacterial Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Nucleotidyltransferases/metabolism , Nucleotidyltransferases/genetics , Nucleotidyltransferases/chemistry , Nucleotidyltransferases/antagonists & inhibitors , Klebsiella Infections/drug therapy , Klebsiella Infections/microbiology , Microbial Sensitivity Tests
2.
Data Brief ; 52: 109918, 2024 Feb.
Article in English | MEDLINE | ID: mdl-38173983

ABSTRACT

Alcohol dehydrogenases (ADHs) catalyze the oxidation of alcohols and reduction of aldehydes and ketones. Primarily ADHs mitigate aldehydes and alcohol toxicity but they may also perform other functions. we listed all ADHs in the genome of strain BD163 of P. brasiliense submitted in www.ncbi.nlm.nih.gov. In total, 11 ADHs or alcohol dehydrogenase catalytic domain-containing proteins from the 4897858-length genome sequence of strain BD163 of P. brasiliense (GenBank JAKNTB000000000.1) were extracted, and when comparing with other strains, it was found that other P. brasiliense strains have similar or slightly different alcohol dehydrogenase capability. Still, other species had varying numbers of ADHs.

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