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IDO-1 Promotes Pulmonary Vascular Remodeling Via Kynurenine Pathway in Pulmonary Arterial Hypertension. [PDF]

open access: yesJ Am Heart Assoc
Cai Z   +17 more
europepmc   +1 more source
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Human Tryptophan Dioxygenase:  A Comparison to Indoleamine 2,3-Dioxygenase

Journal of the American Chemical Society, 2007
In contrast to the diverse superfamily of monooxygenases, there are only two classes of heme-containing dioxygenases in humans. One is tryptophan 2,3 dioxygenase (hTDO), and the other is indoleamine 2,3-dioxygenase (hIDO), both of which catalyze the oxidative degradation of Trp to N-formyl kynurenine.
Dipanwita, Batabyal, Syun-Ru, Yeh
openaire   +2 more sources

N-Benzyl/Aryl Substituted Tryptanthrin as Dual Inhibitors of Indoleamine 2,3-Dioxygenase and Tryptophan 2,3-Dioxygenase.

Journal of Medicinal Chemistry, 2019
Indoleamine 2,3-dioxygenase 1 (IDO1), which catalyzes the initial and rate-limiting step of the kynurenine pathway of tryptophan catabolism, has emerged as a key target in cancer immunotherapy because of its role in enabling cancers to evade the immune ...
Dan Yang   +10 more
semanticscholar   +1 more source

Catechol dioxygenases

Essays in Biochemistry, 1999
Catechol dioxygenases are key enzymes in the metabolism of aromatic rings by soil bacteria. Catechol dioxygenases have been found that participate in the metabolism of halogenated aromatic compounds and, in doing so, play a key role in bioremediation of halogenated pollutants.
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4-Hydroxyphenylpyruvate dioxygenase

Archives of Biochemistry and Biophysics, 2005
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is an Fe(II)-dependent, non-heme oxygenase that catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate. This reaction involves decarboxylation, substituent migration and aromatic oxygenation in a single catalytic cycle.
openaire   +2 more sources

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