Results 1 to 10 of about 25,787 (305)

Functional diversity of bacterial genes associated with aromatic hydrocarbon degradation in anthropogenic dark earth of Amazonia [PDF]

open access: yesPesquisa Agropecuária Brasileira, 2012
The objective of this work was to evaluate the catabolic gene diversity for the bacterial degradation of aromatic hydrocarbons in anthropogenic dark earth of Amazonia (ADE) and their biochar (BC).
Mariana Gomes Germano   +6 more
doaj   +6 more sources

Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation

open access: yesIUCrJ, 2014
Iron(II) and 2-oxoglutarate (2OG)-dependent dioxygenases involved in histone and DNA/RNA demethylation convert the cosubstrate 2OG and oxygen to succinate and carbon dioxide, resulting in hydroxylation of the methyl group of the substrates and subsequent
Cheng Dong, Chao Xu, Cheryl H Arrowsmith
exaly   +3 more sources

OxDBase: a database of oxygenases involved in biodegradation [PDF]

open access: yesBMC Research Notes, 2009
Background Oxygenases belong to the oxidoreductive group of enzymes (E.C. Class 1), which oxidize the substrates by transferring oxygen from molecular oxygen (O2) and utilize FAD/NADH/NADPH as the co-substrate.
Raghava Gajendra PS   +4 more
doaj   +4 more sources

Functional diversity of 2-oxoglutarate/Fe(II)-dependent dioxygenases in plant metabolism [PDF]

open access: yesFrontiers in Plant Science, 2014
Oxidative enzymes catalyze many different reactions in plant metabolism. Among this suite of enzymes are the 2-oxoglutarate/Fe(II)-dependent dioxygenases (2-ODDs). Cytochromes P450 (CYPs) as often considered the most versatile oxidative enzymes in nature,
Scott Cameron Farrow   +1 more
doaj   +3 more sources

Genome-wide analysis of gibberellin-dioxygenases gene family and their responses to GA applications in maize.

open access: yesPLoS ONE, 2021
Gibberellin-dioxygenases genes plays important roles in the regulating plant development. However, Gibberellin-dioxygenases genes are rarely reported in maize, especially response to gibberellin (GA).
Jiabin Ci   +8 more
doaj   +1 more source

Gene Expression during BTEX Biodegradation by a Microbial Consortium Acclimatized to Unleaded Gasoline and a Pseudomonas putida Strain (HM346961) Isolated from It [PDF]

open access: yesPolish Journal of Microbiology, 2017
Pseudomonas putida strain (HM346961) was isolated from a consortium of bacteria acclimatized to unleaded gasoline-contaminated water. The consortium can efficiently remove benzene, toluene, ethylbenzene and xylene (BTEX) isomers, and a similar capability
Jesús A. Morlett Chávez   +4 more
doaj   +1 more source

The Role of Ten-Eleven Translocation Proteins in Inflammation

open access: yesFrontiers in Immunology, 2022
Ten-eleven translocation proteins (TET1-3) are dioxygenases that oxidize 5-methyldeoxycytosine, thus taking part in passive and active demethylation. TETs have shown to be involved in immune cell development, affecting from self-renewal of stem cells and
Christian Gerecke   +3 more
doaj   +1 more source

Structure Elucidation and Biochemical Characterization of Environmentally Relevant Novel Extradiol Dioxygenases Discovered by a Functional Metagenomics Approach

open access: yesmSystems, 2019
The release of synthetic chemical pollutants in the environment is posing serious health risks. Enzymes, including oxygenases, play a crucial role in xenobiotic degradation. In the present study, we employed a functional metagenomics approach to overcome
Chandni Sidhu   +3 more
doaj   +3 more sources

Hydroperoxylation by Hydroxyethylphosphonate Dioxygenase [PDF]

open access: yesJournal of the American Chemical Society, 2009
Hydroxyethylphosphonate dioxygenase (HEPD) catalyzes the O(2)-dependent cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate (2-HEP) to afford hydroxymethylphosphonate (HMP) and formate without input of electrons or use of any organic cofactors. Two mechanisms have been proposed to account for this reaction.
Whitteck, John T.   +2 more
openaire   +2 more sources

Alteration of the Substrate Specificity of the Angular Dioxygenase Carbazole 1,9a-Dioxygenase [PDF]

open access: yesBioscience, Biotechnology, and Biochemistry, 2008
Carbazole 1,9a-dioxygenase (CARDO) consists of terminal oxygenase (CARDO-O) and electron transport components. CARDO can catalyze specific oxygenation for various substrates: angular dioxygenation for carbazole and dibenzo-p-dioxin, lateral dioxygenation for anthracene, and monooxygenation for methylene carbon of fluorene and sulfide sulfur of ...
Hiromasa, Uchimura   +14 more
openaire   +2 more sources

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