cas 13040-58-9, 4(1H)-Pteridinone,2-amino-7-methyl-(8CI,9CI)

Articles about 13040-58-9Total 9 be found

185. Ueber Pterinchemie. Zum Verlauf der katalytischen Reduktion von 6-Methylpterin
The catalytic hydrogenation of 6-methylpterin (I) in neutral or weekly acidic solutions begins, as for the 7-methylpterin, by the thermodynamically controlled reduction of the 7,8-double bond.It is not possible to say, according to our experiments, which double bond, either the 5,6 or the 7,8, is first reduced in strongly acidic solution.However, a 5,8-reduction can be excluded.
Ganguly, Abhoy N.,Sengupta, Pradip K.,Bieri, Jost H.,Visconti, Max
p. 1754 - 1758
(1980)
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FORMATION OF SUBSTITUTED PTERIDINES FROM 5,6-DIAMINOPYRIMIDINES AND N-(ARYLSULFONYL)IMIDAZOLIN-2-ONES
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Zav'yalov, S. I.,Zavozin, A. G.
p. 1355 - 1357
(1981)
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1-HALOGENATED-1-(ACYLAMINO)-2-ALKANONES AS SYNTHONES FOR THE PREPARATION OF QUINOXALINES AND PTERIDINES
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Zav'yalov, S. I.,Ezhova, G. I.,Budkova, T. K.
p. 1459 - 1462
(1984)
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Ueber Pterinchemie. 73. Mitteilung. Zum Verlauf der katalytischen Reduktion von 7-Methylpterin
The catalytic hydrogenation of 7-methylpterin (VII) in a neutral solution occurs first by the reduction of the 7,8-double bond (thermodynamically-controlled reaction) followed by the reduction of the 5,6-double bond.On the contrary, in an acidic medium like CF3COOH, the 5,6-double bond is reduced first (kinetically-controlled reaction).The dihydro-intermermediate then undergoes a -H-rearrangement leading to the formation of the thermodynamically more stable 7-methyl-7,8-dihydropterin (XV) which on further reduction gives 7-methyl-5,6,7,8-tetrahydropterin (VIII).The catalytic reduction of 7-methyl-7,8-dihydropterin (XV) with deuterium gives stereoselectively a sole product with D at C(6) in the equatorial position.
Ganguly, Abboy N.,Sengupta, Pradip K.,Bieri, Jost H.,Viscontini, Max
p. 395 - 401
(1980)
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From hit to lead: De novo design based on virtual screening hits of inhibitors of tRNA-guanine transglycosylase, a putative target of shigellosis therapy
Shigellosis, a bacterial disease, causes the death of more than one million people per year. Extensive studies of Shigella flexneri have recognized tRNA-guanine transglycosylase (TGT, EC 2.4.2.29) as one of the key enzymes involved in the regulation of bacterial virulence. Based on the crystal structure of the Zymomonas mobilis enzyme, we have embarked on the rational design of TGT inhibitors. Herein, we describe the structure-based optimization of hits previously found by virtual screening (see Tables 1-3). For the pteridines, the most potent compound class discovered in a previous virtual screening run, a versatile synthesis could be established giving access to a broad range of substituted derivatives (see Scheme 5). The best ligand in this series, 14, exhibits a Ki = 0.45 μM.
Brenk, Ruth,Gerber, Hans-Dieter,Kittendorf, Jeffrey D.,Garcia, George A.,Reuter, Klaus,Klebe, Gerhard
p. 1435 - 1452
(2007/10/03)