Results 31 to 40 of about 58 (55)

Towards unravelling the structure of an antibiotics-inactivating enzyme – kanamycin kinase [PDF]

open access: yesActa Crystallographica Section A Foundations of Crystallography, 1996
W. -C. Hon   +3 more
openaire   +1 more source

Identification of Distinct Interacting Proteins of Giardia lamblia Centrins Using Yeast Two‐Hybrid Assays

open access: yesJournal of Eukaryotic Microbiology, Volume 73, Issue 4, July/August 2026.
ABSTRACT Giardia lamblia, a protozoan parasite that causes diarrhea in humans, contains two centrins implicated in cellular morphology and cell division. To identify proteins interacting with each G. lamblia centrin (GlCent), we performed a yeast two‐hybrid assay.
Mee Young Shin   +2 more
wiley   +1 more source

Substrate Specificity of B12‐Depedent Ribonucleotide Reductases: Biotechnology and Metabolic Implications

open access: yesChemBioChem, Volume 27, Issue 11, 15 June 2026.
Ribonucleotide reductases (RNRs) are valuable biocatalysts for the biosynthesis of non‐natural deoxyribonucleotide, relevant in fields like medical science and synthetic biology. In this study, we explore the substrate spectrum of two thermostable RNRs and discuss their implications for nucleotide metabolism and biocatalytical applications ...
Lobna Eltoukhy, Christoph Loderer
wiley   +1 more source
Some of the next articles are maybe not open access.

Kanamycin triggered nanozyme for homogeneous and amplified colorimetric detection of T4 polynucleotide kinase

Talanta, 2023
It is of significance to develop efficient methods for detecting the activity of T4 polynucleotide kinase (T4 PNK) due to its essential role in the modulation of different life activities. In this work, we constructed a novel nanozyme using Kanamycin (KANA) as a trigger for the [Fe(CN)6]3- coordinated Cu2(OH)3NO3 (Cu2(OH)3NO3/[Fe(CN)6]3-) nanorods, and
Xiuming Wu, Guang-Li Wang
exaly   +3 more sources

Kanamycin kinase

1997
Dietmar Schomburg, Dörte Stephan
exaly   +2 more sources

Catalytic Mechanism of Enterococcal Kanamycin Kinase (APH(3‘)-IIIa):  Viscosity, Thio, and Solvent Isotope Effects Support a Theorell−Chance Mechanism

Biochemistry, 1996
Bacterial resistance to the aminoglycoside antibiotics is manifested primarily through the production of enzymes which covalently modify these drugs. The Enterococci and Staphylococci produce an ATP-dependent kinase, APH(3')-IIIa, which phosphorylates such antibiotics as kanamycin, amikacin, and neomycin, and this enzyme shows a Theorell-Chance kinetic
G A, McKay, G D, Wright
openaire   +2 more sources

Crystallographic studies on two structures of a kanamycin kinase: a Mg-AMPPNP and a Mg-ADP complex.

1998
3',5"-aminoglycoside phosphotransferase type IIIa (APH(3')-IIIa) belongs to a family of bacterial enzymes that phosphorylate the aminoglycoside antibiotics. The modified antibiotics are rendered ineffective due to a lowered affinity for their targets in the bacterial cells.
openaire   +1 more source

Construction of a self-sufficient DNA circuit for amplified detection of kanamycin

Food Chemistry, 2023
Chuanyi Liu   +2 more
exaly  

Home - About - Disclaimer - Privacy