Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Expanding Aminoglycoside Resistance Enzyme Regiospecificity by Mutation and Truncation.

Biochemistry - 11 Oct 2016

Holbrook Selina Y L, Garneau-Tsodikova Sylvie

Abstract excerpt

Aminoglycosides (AGs) are broad-spectrum antibiotics famous for their antibacterial activity against Gram-positive and Gram-negative bacteria, as well as mycobacteria. In the United States, the most prescribed AGs, including amikacin (AMK), gentamicin (GEN), and tobramycin (TOB), are vital components of the treatment for resistant bacterial infections. Arbekacin (ABK), a semisynthetic AG, is widely used for the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Mass Spectrometry
Share to Acetylation
Share to Acetyltransferases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Aminoglycosides

Share to Kinetics

Share to Phosphotransferases

Share to Spectrophotometry, Ultraviolet

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 27618454
DOI: 10.1021/acs.biochem.6b00770
PMCID: PMC5174979

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expanding Aminoglycoside Resistance Enzyme Regiospecificity by Mutation and Truncation.PMID 27618454Read ↗

Mycobacterial Aminoglycoside Acetyltransferases: A Little of Drug Resistance, and a Lot of Other RolesSemantic proximity Read ↗

Characterization of Substrate Distribution and Functional Implication of Lysine Acylations in Staphylococcus aureusSemantic proximity Read ↗

Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT familySemantic proximity Read ↗

A novel chromosomal aminoglycoside 6′-N-acetyltransferase, AAC(6′)-Io, confers resistance to multiple aminoglycosides identified from Bacillus cereusSemantic proximity Read ↗

Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB.Semantic proximity Read ↗

Development of Peptides that Inhibit Aminoglycoside-Modifying Enzymes and β-Lactamases for Control of Resistant BacteriaSemantic proximity Read ↗

Aminoglycoside phosphotransferases: proteins, structure, and mechanismSemantic proximity Read ↗

Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6')-Ib and its bifunctional, fluoroquinolone-active AAC(6')-Ib-cr variant.Semantic proximity Read ↗

Fluoroquinolone-modifying enzyme: a new adaptation of a common aminoglycoside acetyltransferase.Semantic proximity Read ↗

Identification and characterization of a novel chromosomal aminoglycoside 3’-O-phosphotransferase, APH(3′)-Id, from Kluyvera intermedia DW18 isolated from the sewage of an animal farmSemantic proximity Read ↗

Functional characterization of a novel aminoglycoside phosphotransferase, APH(9)-Ic, and its variant from Stenotrophomonas maltophiliaSemantic proximity Read ↗

Potential Role of Lysine Acetylation in Antibiotic Resistance of Escherichia coliSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.