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Mutagenicities of indole and 30 derivatives after nitrite treatment

Mutagenicities of indole and 30 derivatives after nitrite treatment. Ochiai, Masako; Wakabayashi, Keiji; Sugimura, Takashi; Nagao, Minako (Carcinog. Div., Natl. Cancer Cent. Res. Inst., Tokyo 104, Japan). Mutat. Res., 172(3), 189-97 (English) 1986. CODEN: MUREAV. ISSN: 0027-5107. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Indole (I) [120-72-9] and 7 derivs., L- [73-22-3] and D-tryptophan [153-94-6] and 9 derivs., and norharman [244-63-3] and 11 derivs. were tested for mutagenicity to Salmonella typhimurium TA100 and TA98 after nitrite treatment. 1-Methylindole [603-76-9], which is present in cigaret smoke condensate was the most mutagenic to TA100 without S9 mix after nitrite treatment, inducing 615,000 revertants/mg. 2-Methylindole [95-20-5], 1-methyl-DL-tryptophan [26988-72-7], harmaline [304-21-2], and (-)-(1S,3S)-1,2-dimethyl-1,2,3,4-tetrahydro-b-carboline-3-carboxylic acid [54193-05-4] also showed strong mutagenicity after nitrite treatment, inducing 129,000, 184,000, 103,000, and 197,000 revertants/mg, resp. These mutagenic potencies were comparable with those of benzo[a]pyrene, 3-methyolcholanthrene and 2-amino-9H-pyrido[2,3-b]indole. Of 31 compds. tested, 22 were mutagenic after nitrite treatment. Since various indole compds. are ubiquitous in our environment, esp. in plants, the presence of their mutagenicities after nitrite treatment warrants further studies, including those on their in vivo carcinogenicities.

1-Methyl-DL-tryptophan, b-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and b-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase

1-Methyl-DL-tryptophan, b-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and b-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Cady, Susan G.; Sono, Masanori (Dep. Chem. Biochem., Univ. South Carolina, Columbia, SC 29208, USA). Arch. Biochem. Biophys., 291(2), 326-33 (English) 1991. CODEN: ABBIA4. ISSN: 0003-9861. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The tryptophan (Trp) analogs, 1-methyl-DL-Trp, b-(3-benzofuranyl)-DL-alanine (the O analog of Trp), and b-(3-benzo[b]thienyl)-DL-alanine (the S analog of Trp), each of which has a substitution at the indole N atom, were found to be the 1st examples of potent substrate analog competitive inhibitors (Ki, 7-70 mM) with respect to the substrates, D-Trp and L-Trp, for rabbit small intestinal indoleamine 2,3-dioxygenase. Binding studies using optical absorption and CD spectroscopy demonstrated that these 3 inhibitors caused spectral changes upon binding to the native ferric, ferrous, ferrous-CO, and ferrous-NO enzymes. 26988-72-7 and 72071-49-9 are also in the experiment. Such spectral effects of 1-methyl-DL-Trp on all of these enzyme derivs. were similar to those caused by L-Trp, whereas the S and the O analogs of Trp exhibited relatively small effects except for those obsd. for the S analog with CD spectroscopy. Each of these 3 Trp analog inhibitors competed with L-Trp for the ferrous-CO enzyme, a model for the ferrous-O2 enzyme. The present findings demonstrate that, although substitution of a Me group for the H atom on the indole N atom or of a more electron-inductive S or O atom for the indole N atom did not prevent the binding of the resulting Trp analog to indoleamine 2,3-dioxygenase, the free form of the indole N base is an important phys. and/or electronic structural requirement for Trp to be metabolized by the enzyme. The inability of 1-methyl-Trp to serve as a substrate for the dioxygenase supports a view that singlet O is not the reactive O species involved in the dioxygenation of Trp by the enzyme. .