Literature summary for 1.14.14.47 extracted from

Buddha, M.R.; Tao, T.; Parry, R.J.; Crane, B.R.
Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase (2004), J. Biol. Chem., 279, 49567-49570.

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Activating Compound

Activating Compound	Comment	Organism	Structure
tryptophan	stimulates oxidation of substrate L-arginine. Tryptophan or a derivative thereof may bind in the enzyme's pterin site, participate in arginine oxidation, and become nitrated at the 4-position	Deinococcus radiodurans

Organism

Organism	UniProt	Comment	Textmining
Deinococcus radiodurans	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the complex between enzyme and the unusual tryptophanyl-tRNA synthetase TrpRS II catalyzes the regioselective nitration of tryptophan at the 4-position. The enzyme alone will catalyze 4-nitrotryptophan production, but yields are significantly enhanced by TrpRS II and ATP. 4-Nitro-tryptophan formation exhibits saturation behavior with tryptophan and is completely inhibited by the addition of the mammalian nitric-oxide synthase cofactor (6R)-5,6,7,8-tetrahydro-L-biopterin	Deinococcus radiodurans	?	-	?

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Release 2023.1 (January 2023)