73637-65-7Relevant academic research and scientific papers
N 1-fluoroalkyltryptophan analogues: Synthesis and in vitro study as potential substrates for indoleamine 2,3-dioxygenase
Henrottin, Jean,Zervosen, Astrid,Lemaire, Christian,Sapunaric, Frédéric,Laurent, Sophie,Van Den Eynde, Benoit,Goldman, Serge,Plenevaux, Alain,Luxen, André
, p. 260 - 265 (2015)
Indoleamine 2,3-dioxygenase (hIDO) is an enzyme that catalyzes the oxidative cleavage of the indole ring of l-tryptophan through the kynurenine pathway, thereby exerting immunosuppressive properties in inflammatory and tumoral tissues. The syntheses of 1-(2-fluoroethyl)-tryptophan (1-FETrp) and 1-((1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl)methyl)-tryptophan, two N1-fluoroalkylated tryptophan derivatives, are described here. In vitro enzymatic assays with these two new potential substrates of hIDO show that 1-FETrp is a good and specific substrate of hIDO. Therefore, its radioactive isotopomer, 1-[18F]FETrp, should be a molecule of choice to visualize tumoral and inflammatory tissues and/or to validate new potential inhibitors.
Human indoleamine 2,3-dioxygenase-2 has substrate specificity and inhibition characteristics distinct from those of indoleamine 2,3-dioxygenase-1
Pantouris, Georgios,Serys, Martynas,Yuasa, Hajime J.,Ball, Helen J.,Mowat, Christopher G.
, p. 2155 - 2163 (2014/12/10)
Indoleamine 2,3-dioxygenase-2 (IDO2) is one of three enzymes (alongside tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase (IDO1)) that catalyse dioxygenation of l-tryptophan as the first step in the kynurenine pathway. Despite the reported expres
OXIDATIVE TRANSFORMATION OF TRYPTOPHAN TO 5-HYDROXY-N-FORMYLKYNURENINE
Nakagawa, Masako,Yokoyama, Yukio,Kato, Shiro,Hino, Tohru
, p. 59 - 62 (2007/10/02)
Dye-sensitized photooxygenation of L-tryptophan in an alkaline phosphate buffer followed by NaBH4 reduction afforded 3a,5-dihydroxypyrroloindole 5 which readily underwent air oxidation to give 5-hydroxy-N-formylkynurenine 6a.
