منابع مشابه
Heme-dependent dioxygenases in tryptophan oxidation.
L-Tryptophan is an essential amino acid for mammals. It is utilized not only for protein synthesis but also for the biosynthesis of serotonin and melatonin by the serotonin pathway as well as nicotinamide adenine dinucleotide by the kynurenine pathway. Although the kynurenine pathway is responsible for the catabolism of over 90% of l-tryptophan in the mammalian intracellular and extracellular p...
متن کاملPlant phenolics affect oxidation of tryptophan.
The effect of berry phenolics such as anthocyanins, ellagitannins, and proanthocyanidins from raspberry (Rubus idaeus), black currant (Ribes nigrum), and cranberry (Vaccinium oxycoccus) and byproducts of deoiling processes rich in phenolics such as rapeseed (Brassica rapa L.), camelina (Camelina sativa), and soy (Glycine max L.) as well as scots pine bark (Pinus sylvestris) was investigated in ...
متن کاملOxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase.
The family of haem dioxygenases catalyse the initial oxidative cleavage of L-tryptophan to N-formylkynurenine, which is the first, rate-limiting, step in the L-kynurenine pathway. In the present paper, we discuss and compare structure and function across the family of haem dioxygenases by focusing on TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase), including a review of r...
متن کاملTryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation.
Myeloperoxidase, released by activated phagocytes, forms reactive oxidants by catalysing the reaction of halide and pseudo-halide ions with H(2)O(2). These oxidants have been linked to tissue damage in a range of inflammatory diseases. With physiological levels of halide and pseudo-halide ions, similar amounts of HOCl (hypochlorous acid) and HOSCN (hypothiocyanous acid) are produced by myeloper...
متن کاملHeme-dependent Tryptophan Oxidation: Mechanistic Studies on Tryptophan 2,3-Dioxygenase and MauG
Hemoenzymes are prevalent in nature and participate in a wide range of biological activities. Frequently, high-valence iron intermediates are involved in the catalytic events of these enzymes, especially when the activation of peroxide or dioxygen is involved. Building on the fundamental framework of iron-oxygen chemistry, the mechanistic understandings of these enzymes and their reactive inter...
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ژورنال
عنوان ژورنال: Pediatric Research
سال: 1967
ISSN: 0031-3998,1530-0447
DOI: 10.1203/00006450-196709000-00005