Results 21 to 30 of about 63,041 (289)

Nature’s Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases

open access: yesACS Catalysis, 2020
Iron is an especially important redox-active cofactor in biology because of its ability to mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth-abundant transition metal for the insertion of oxygen atoms into organic ...
N. Dunham, F. Arnold
semanticscholar   +1 more source

Transcriptomic Analysis of Rhodococcus opacus R7 Grown on o-Xylene by RNA-Seq

open access: yesFrontiers in Microbiology, 2020
Xylenes are considered one of the most common hazardous sources of environmental contamination. The biodegradation of these compounds has been often reported, rarer the ability to oxidize the ortho-isomer.
Jessica Zampolli   +5 more
doaj   +1 more source

Role of Structural Dynamics in Selectivity and Mechanism of Non-heme Fe(II) and 2-Oxoglutarate-Dependent Oxygenases Involved in DNA Repair

open access: yesACS Central Science, 2020
AlkB and its human homologue AlkBH2 are Fe(II)- and 2-oxoglutarate (2OG)-dependent oxygenases that repair alkylated DNA bases occurring as a consequence of reactions with mutagenic agents.

semanticscholar   +1 more source

Enzymology of Vertebrate Carotenoid Oxygenases

open access: yesBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 2020
Mammals and higher vertebrates including humans have only three members of the carotenoid cleavage dioxygenase family of enzymes. This review focuses on the two that function as carotenoid oxygenases.
E. Harrison, R. Kopec
semanticscholar   +1 more source

Enzyme Kinetics of Organic Contaminant Oxygenations

open access: yesCHIMIA, 2020
Enzymatic oxygenations initiate biodegradation processes of many organic soil and water contaminants. Even though many biochemical aspects of oxygenation reactions are well-known, quantifying rates of oxidative contaminant removal as well as the extent ...
Charlotte E. Bopp   +2 more
doaj   +1 more source

Design principles for site-selective hydroxylation by a Rieske oxygenase

open access: yesNature Communications, 2022
SxtT and GxtA are Rieske oxygenases that are involved in paralytic shellfish toxin biosynthesis and catalyze monohydroxylation reactions at different positions on the toxin scaffold.
Jianxin Liu   +6 more
doaj   +1 more source

Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators

open access: yesBiochemical Society Transactions, 2020
Fe(II)/2-oxoglutarate (2OG)-dependent oxygenases are a conserved enzyme class that catalyse diverse oxidative reactions across nature. In humans, these enzymes hydroxylate a broad range of biological substrates including DNA, RNA, proteins and some ...
Sally C. Fletcher, M. Coleman
semanticscholar   +1 more source

ENGINEERING NON-HEME MONO- AND DIOXYGENASES FOR BIOCATALYSIS

open access: yesComputational and Structural Biotechnology Journal, 2012
Oxygenases are ubiquitous enzymes that catalyze the introduction of one or two oxygen atoms to unreactive chemical compounds. They require reduction equivalents from NADH or NADPH and comprise metal ions, metal ion complexes, or coenzymes in their active
Adi Dror, Ayelet Fishman
doaj   +3 more sources

Unraveling the Microbial Interactions and Metabolic Potentials in Pre- and Post-treated Sludge from a Wastewater Treatment Plant Using Metagenomic Studies

open access: yesFrontiers in Microbiology, 2017
Sewage waste represents an ecosystem of complex and interactive microbial consortia which proliferate with different kinetics according to their individual genetic as well as metabolic potential. We performed metagenomic shotgun sequencing on Ion-Torrent
Chandni Sidhu   +3 more
doaj   +1 more source

Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans

open access: yesScientific Reports, 2022
The JmjC family of 2-oxoglutarate dependent oxygenases catalyse a range of hydroxylation and demethylation reactions in humans and other animals. Jumonji domain-containing 7 (JMJD7) is a JmjC (3S)-lysyl-hydroxylase that catalyses the modification of ...
Rasheduzzaman Chowdhury   +5 more
doaj   +1 more source

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