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<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Current Protein &amp; Peptide Science</journal-id><journal-title-group><journal-title xml:lang="en">Current Protein &amp; Peptide Science</journal-title><trans-title-group xml:lang="ru"><trans-title>Current Protein &amp; Peptide Science</trans-title></trans-title-group></journal-title-group><issn publication-format="print">1389-2037</issn><issn publication-format="electronic">1875-5550</issn><publisher><publisher-name xml:lang="en">Bentham Science</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">645647</article-id><article-id pub-id-type="doi">10.2174/0113892037278814231226104509</article-id><article-categories><subj-group subj-group-type="toc-heading"><subject>Life Sciences</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Combating Aminoglycoside Resistance: From Structural and Functional Characterisation to Therapeutic Challenges with RKAAT</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Otun</surname><given-names>Sarah</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Graca</surname><given-names>Richard</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Achilonu</surname><given-names>Ikechukwu</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib></contrib-group><aff id="aff1"><institution>Department of Molecular and Cell Biology, Protein Structure-function Unit, University of Witwatersrand</institution></aff><pub-date date-type="pub" iso-8601-date="2024-06-01" publication-format="electronic"><day>01</day><month>06</month><year>2024</year></pub-date><volume>25</volume><issue>6</issue><issue-title xml:lang="ru"/><fpage>454</fpage><lpage>468</lpage><history><date date-type="received" iso-8601-date="2025-01-11"><day>11</day><month>01</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2024, Bentham Science Publishers</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="en">Bentham Science Publishers</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/></permissions><self-uri xlink:href="https://journals.eco-vector.com/1389-2037/article/view/645647">https://journals.eco-vector.com/1389-2037/article/view/645647</self-uri><abstract xml:lang="en"><p id="idm46466589579312">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 continu</p></abstract><kwd-group xml:lang="en"><kwd>Adenylyl transferase</kwd><kwd>aminoglycoside antibiotics</kwd><kwd>antibiotic resistance</kwd><kwd>healthcare-associated infections</kwd><kwd>Klebsiella pneumoniae</kwd><kwd>recombinant</kwd><kwd>Klebsiella pneumoniae Aminoglycoside</kwd><kwd>(3) (9) adenylyl transferase (RKAAT).</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Mancuso, G.; Midiri, A.; Gerace, E.; Biondo, C. Bacterial antibiotic resistance: The most critical pathogens. Pathogens, 2021, 10(10), 1310. doi: 10.3390/pathogens10101310 PMID: 34684258</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Darby, E.M.; Trampari, E.; Siasat, P.; Gaya, M.S.; Alav, I.; Webber, M.A.; Blair, J.M.A. Molecular mechanisms of antibiotic resistance revisited. Nat. Rev. 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