Results 61 to 70 of about 10,817 (260)

Enhanced production of alkane hydroxylase from Penicillium chrysogenum SNP5 (MTCC13144) through feed-forward neural network and genetic algorithm

open access: yesAMB Express, 2022
Alkane hydroxylase (AlkB), a membrane-bound enzyme has high industrial demand; however, its economical production remains challenging due to its intrinsic nature and co-factor dependency.
Satyapriy Das, Sangeeta Negi
doaj   +1 more source

Alkane hydroxylase genes in psychrophile genomes and the potential for cold active catalysis. [PDF]

open access: yes, 2014
BackgroundPsychrophiles are presumed to play a large role in the catabolism of alkanes and other components of crude oil in natural low temperature environments.
Bowman, Jeff S, Deming, Jody W
core   +2 more sources

A chemical genetics analysis of the roles of bypass polymerase DinB and DNA repair protein AlkB in processing N2-alkylguanine lesions in vivo. [PDF]

open access: yesPLoS ONE, 2014
DinB, the E. coli translesion synthesis polymerase, has been shown to bypass several N2-alkylguanine adducts in vitro, including N2-furfurylguanine, the structural analog of the DNA adduct formed by the antibacterial agent nitrofurazone. Recently, it was
Nidhi Shrivastav   +7 more
doaj   +1 more source

Mechanism of Repair of Acrolein- and Malondialdehyde-Derived Exocyclic Guanine Adducts by the α-Ketoglutarate/Fe(II) Dioxygenase AlkB [PDF]

open access: yes, 2014
The structurally related exocyclic guanine adducts α-hydroxypropano-dG (α-OH-PdG), γ-hydroxypropano-dG (γ-OH-PdG), and M[subscript 1]dG are formed when DNA is exposed to the reactive aldehydes acrolein and malondialdehyde (MDA).
Delaney, James C.   +8 more
core   +3 more sources

Schizosaccharomyces pombe Ofd2 is a nuclear 2-oxoglutarate and iron dependent dioxygenase interacting with histones. [PDF]

open access: yesPLoS ONE, 2011
2-Oxoglutarate (2OG) dependent dioxygenases are ubiquitous iron containing enzymes that couple substrate oxidation to the conversion of 2OG to succinate and carbon dioxide.
Hanne Korvald   +6 more
doaj   +1 more source

Characterization and Transcriptional Regulation of n-Alkane Hydroxylase Gene Cluster of Rhodococcus jostii RHA1

open access: yesMicroorganisms, 2019
Gram-positive actinomycete Rhodococcus jostii RHA1 is able to grow on C10 to C19 n-alkanes as a sole source of carbon and energy. To clarify, the n-alkane utilization pathway—a cluster of 5 genes (alkBrubA1A2BalkU) which appeared to be involved in ...
Namiko Gibu   +4 more
doaj   +1 more source

A nonradioactive restriction enzyme-mediated assay to detect DNA repair by Fe(II)/2-oxoglutarate-dependent dioxygenase [PDF]

open access: yes, 2014
The Escherichia coli DNA repair enzyme AlkB belongs to the Fe(II)/2-oxoglutarate-dependent dioxygenase family. It removes methyl groups from 1-methyl adenine (1-meA) and 3-methyl cytosine (3-meC) lesions present in single-stranded DNA by oxidative ...
K, Naveena, Roy, Anindya, S, Gururaj
core   +1 more source

RecA stimulates AlkB-mediated direct repair of DNA adducts [PDF]

open access: yesNucleic Acids Research, 2016
The Escherichia coli AlkB protein is a 2-oxoglutarate/Fe(II)-dependent demethylase that repairs alkylated single stranded and double stranded DNA. Immunoaffinity chromatography coupled with mass spectrometry identified RecA, a key factor in homologous recombination, as an AlkB-associated protein.
Naveena Kodipelli   +4 more
openaire   +4 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   +1 more source

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

open access: yes, 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.
Atmore, Kyle Aaquil   +8 more
core   +2 more sources

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