Results 21 to 30 of about 13,374 (242)
Structural basis for endoperoxide-forming oxygenases
Endoperoxide natural products are widely distributed in nature and exhibit various biological activities. Due to their chemical features, endoperoxide and endoperoxide-derived secondary metabolites have attracted keen attention in the field of natural ...
Takahiro Mori, Ikuro Abe
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OxDBase: a database of oxygenases involved in biodegradation
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
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Rieske-type two-component vanillate O-demethylases (VanODs) catalyze conversion of the lignin-derived monomer vanillate into protocatechuate in several bacterial species. Currently, VanODs have received attention because of the demand of effective lignin
Raúl A. Donoso +4 more
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Most polyunsaturated fatty acids have the minimal 1,4-cis,cis-pentadiene configuration to be oxygenated into a conjugated diene hydroperoxide. This product is usually reduced into the corresponding hydroxy derivative by cell glutathione peroxidases.
Lagarde Michel
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Non-heme iron and α-ketoglutarate-dependent (Fe/αKG) oxygenases have attracted attention for their application as biocatalysts due to their flexibility and high efficiency.
Hui Tao +6 more
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The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression
Loss of NOX4 in HCC tumor cells induces metabolic reprogramming in a Nrf2/MYC‐dependent manner to promote HCC progression. Abstract Background and Aims The NADPH oxidase NOX4 plays a tumor‐suppressor function in HCC. Silencing NOX4 confers higher proliferative and migratory capacity to HCC cells and increases their in vivo tumorigenic potential in ...
Irene Peñuelas‐Haro +14 more
wiley +1 more source
Heme is essential for respiration across all domains of life. However, heme accumulation can lead to toxicity if cells are unable to either degrade or export heme or its toxic by-products.
Lisa J. Lojek +7 more
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Bacillus subtilis HmoB is a heme oxygenase with a novel structure [PDF]
Iron availability is limited in the environment and mostbacteria have developed a system to acquire iron from hosthemoproteins. Heme oxygenase plays an important role bydegrading heme group and releasing the essential nutrientiron.
Seonghun Park, Sarah Choi, Jungwoo Choe
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Non-heme iron and α-ketoglutarate (αKG) oxygenases play a major role in fungal meroterpenoid biosynthesis, but their mechanism remains elusive. Here the authors present crystal structures of two oxygenases, AusE and PrhA, which provide insights into the ...
Yu Nakashima +7 more
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Stress-inducible heme oxygenase-1 (HO-1) catalyzes the oxidative cleavage of heme yielding biliverdin, ferrous iron, and carbon monoxide (CO). Heme oxygenase activity has been attributed to antioxidant defense via the redox cycling system of biliverdin ...
David Stucki +9 more
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