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Endocannabinoids and their oxygenation by cyclo-oxygenases, lipoxygenases and other oxygenases

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2015
The naturally occurring mammalian endocannabinoids possess biological attributes that extend beyond interaction with cannabinoid receptors. These extended biological properties are the result of oxidative metabolism of the principal mammalian endocannabinoids arachidonoyl ethanolamide (anandamide; A-EA) and 2-arachidonoylglycerol (2-AG).
Urquhart, P   +2 more
openaire   +2 more sources

Heme-Containing Oxygenases

Chemical Reviews, 1996
John H. Dawson   +2 more
exaly   +3 more sources

Homogeneous Oxygenase Catalysis

Chemical Reviews, 2018
Oxygenases-catalyzed reductive activation of molecular oxygen and incorporation of O atoms into an organic molecule is undoubtedly one of the most attractive research areas. Typically, these oxygenation reactions proceed with high selectivity and reactivity, which is seldom found in its "biomimetic" chemocatalytic counterparts.
Yujie Liang   +3 more
openaire   +2 more sources

Heme-Oxygenase-1

Antioxidants & Redox Signaling, 2020
This Forum issue “Heme Oxygenase” (HO) includes original research articles and reviews that are aimed at understanding the role of HO-1 in several pathophysiological conditions, specially addressing those involving inflammation and oxidative damage.
openaire   +3 more sources

Oxygenases, Thwarted Oxygenases, and Oxygen-dependent Halogenases

2022
Oxygenases, both flavin-dependent and iron-dependent, act on all classes of natural products, often late in scaffold maturation, to introduce oxygen functional groups, including hydroxyl and epoxide groups. The hydroxyl groups then function as nucleophiles for alkylations, acylations, and glycosylations.
openaire   +1 more source

Heme Oxygenase and the Kidney

DNA and Cell Biology, 2002
Heme plays a significant pathogenic role in several diseases involving the kidney. The cellular content of heme, derived either from the delivery of filtered heme proteins such as hemoglobin and myoglobin, or from the breakdown of ubiquitous intracellular heme proteins, is regulated via the heme oxygenase enzyme system.
Nathalie, Hill-Kapturczak   +2 more
openaire   +2 more sources

The mechanism of heme oxygenase

Current Opinion in Chemical Biology, 2000
Major advances have been made in determining the structure of heme oxygenase and the relationship between its structure and catalytic activity. The nature of the first step in the reaction sequence, heme alpha-meso-hydroxylation, is now clear, although the mechanisms that control the alpha-regiospecificity remain elusive. Hypothetical mechanisms can be
openaire   +2 more sources

Heme oxygenase-1 and heme oxygenase-2 expression in bruises

Forensic Science, Medicine, and Pathology, 2015
The first step in catabolism of hemoglobin in a bruise is performed by the enzyme heme oxygenase, which produces biliverdin that is then reduced to bilirubin. The development of yellow coloration in bruises can be attributed to local accumulation of degradation products of hemoglobin, including bilirubin, but it is not clear why there is a delay before
Neil E I, Langlois   +3 more
openaire   +2 more sources

2-Oxoglutarate-Dependent Oxygenases

Annual Review of Biochemistry, 2018
2-Oxoglutarate (2OG)-dependent oxygenases (2OGXs) catalyze a remarkably diverse range of oxidative reactions. In animals, these comprise hydroxylations and N-demethylations proceeding via hydroxylation; in plants and microbes, they catalyze a wider range including ring formations, rearrangements, desaturations, and halogenations.
Islam, M   +4 more
openaire   +2 more sources

Bacterial Heme Oxygenases

Antioxidants & Redox Signaling, 2004
The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme
openaire   +2 more sources

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