Results 21 to 30 of about 13,613 (257)

OxDBase: a database of oxygenases involved in biodegradation

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   +1 more source

Métabolisme oxygéné des acides gras polyinsaturés et fonction dans les cellules sanguines et vasculaires1

open access: yesOléagineux, Corps gras, Lipides, 2011
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
doaj   +1 more source

Structural basis for endoperoxide-forming oxygenases

open access: yesBeilstein Journal of Organic Chemistry, 2022
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
doaj   +1 more source

Identification of a Phylogenetically Divergent Vanillate O-Demethylase from Rhodococcus ruber R1 Supporting Growth on Meta-Methoxylated Aromatic Acids

open access: yesMicroorganisms, 2022
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
doaj   +1 more source

Bacillus subtilis HmoB is a heme oxygenase with a novel structure [PDF]

open access: yesBMB Reports, 2012
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
doaj   +1 more source

Chlamydomonas reinhardtii LFO1 Is an IsdG Family Heme Oxygenase

open access: yesmSphere, 2017
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
doaj   +1 more source

Molecular insights into the unusually promiscuous and catalytically versatile Fe(II)/α-ketoglutarate-dependent oxygenase SptF

open access: yesNature Communications, 2022
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
doaj   +1 more source

Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis

open access: yesNature Communications, 2018
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
doaj   +1 more source

Endogenous Carbon Monoxide Signaling Modulates Mitochondrial Function and Intracellular Glucose Utilization: Impact of the Heme Oxygenase Substrate Hemin

open access: yesAntioxidants, 2020
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
doaj   +1 more source

Heme Oxygenase-Like Metalloenzymes. [PDF]

open access: yesAnnu Rev Biochem
Heme oxygenase (HO)-like metalloenzymes are an emerging protein superfamily diverse in reaction outcome and mechanism. Found primarily in bacterial biosynthetic pathways, members conserve a flexible protein scaffold shared with the heme catabolic enzyme, HO, and a set of metal-binding residues.
Pope SR   +6 more
europepmc   +4 more sources

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