Results 1 to 10 of about 10,203 (251)

Structure and mechanism of the alkane-oxidizing enzyme AlkB

open access: yesNature Communications, 2023
Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle.
Jianxiu Zhang, , Rachel Narehood Austin
exaly   +5 more sources

Structural Analysis of the AlkB Family in Poultry [PDF]

open access: yesAnimals
The objective of this study was to identify the AlkB family genes in poultry using bioinformatics, and to explore their molecular characteristics, evolutionary relationships, and expression patterns to clarify their potential functions in poultry.
Yuling Niu   +6 more
doaj   +3 more sources

Viral AlkB proteins repair RNA damage by oxidative demethylation [PDF]

open access: goldNucleic Acids Research, 2008
Bacterial and mammalian AlkB proteins are iron(II)- and 2-oxoglutarate-dependent dioxygenases that reverse methylation damage, such as 1-methyladenine and 3-methylcytosine, in RNA and DNA. An AlkB-domain is encoded by the genome of numerous single-stranded, plant-infecting RNA viruses, the majority of which belong to the Flexiviridae family.
Valerian Dolja, Pål Ø Falnes
exaly   +4 more sources

The Use of a Combination of alkB Primers to Better Characterize the Distribution of Alkane-Degrading Bacteria. [PDF]

open access: goldPLoS ONE, 2013
The alkane monooxygenase AlkB, which is encoded by the alkB gene, is a key enzyme involved in bacterial alkane degradation. To study the alkB gene within bacterial communities, researchers need to be aware of the variations in alkB nucleotide sequences ...
Diogo Jurelevicius   +4 more
doaj   +3 more sources

Molecular Detection and Phylogenetic Analysis of the alkB Gene in Klebsiella oxytoca Strains Isolated from the Gut of Tenebrio molitor [PDF]

open access: goldThe Scientific World Journal
The challenge in polystyrene disposal has caused researchers to look for urgent innovative and ecofriendly solutions for plastic degradation. Some insects have been reported to use polystyrene as their sole carbon source, and this has been linked to the ...
Tsitsi Lynn Mupamhadzi   +3 more
doaj   +2 more sources

An Overview of the Electron-Transfer Proteins That Activate Alkane Monooxygenase (AlkB) [PDF]

open access: goldFrontiers in Microbiology, 2022
Alkane-oxidizing enzymes play an important role in the global carbon cycle. Alkane monooxygenase (AlkB) oxidizes most of the medium-chain length alkanes in the environment. The first AlkB identified was from P.
Shoshana C. Williams   +1 more
doaj   +2 more sources

Human AlkB Homolog ABH8 Is a tRNA Methyltransferase Required for Wobble Uridine Modification and DNA Damage Survival [PDF]

open access: yesMolecular and Cellular Biology, 2010
tRNA nucleosides are extensively modified to ensure their proper function in translation. However, many of the enzymes responsible for tRNA modifications in mammals await identification.
Tsz Yan Clement Chan   +2 more
exaly   +4 more sources

Genomic analysis of Acinetobacter baumannii DUEMBL6 reveals diesel bioremediation potential and biosafety concerns. [PDF]

open access: yesPLoS ONE
This study investigates the bioremediation potential of bacterial isolates from diesel-contaminated soils in Dhaka, Bangladesh. A total of 34 morphologically distinct bacterial strains were isolated from hydrocarbon-polluted sites, with Acinetobacter ...
Nizam Uddin   +8 more
doaj   +2 more sources

Human ALKBH4 interacts with proteins associated with transcription. [PDF]

open access: yesPLoS ONE, 2012
The Fe(II)- and 2-oxoglutarate (2OG)-dependent dioxygenase AlkB from E. coli is a demethylase which repairs alkyl lesions in DNA, as well as RNA, through a direct reversal mechanism. Humans possess nine AlkB homologs (ALKBH1-8 and FTO). ALKBH2 and ALKBH3
Linn G Bjørnstad   +5 more
doaj   +6 more sources

NAIL-MS reveals the repair of 2-methylthiocytidine by AlkB in E. coli

open access: yesNature Communications, 2019
Bacterial tRNA is modified by thiolation of nucleosides. Here the authors identify 2-methylthiocytidine in bacterial tRNA using nucleic acid isotope labeling coupled mass spectrometry.
Stefanie M Kellner
exaly   +2 more sources

Home - About - Disclaimer - Privacy