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Takai, K.; Hayaishi, O.: Purification and properties of tryptophan side chain oxidase types I and II from Pseudomonas. Methods Enzymol., 142, 195–217 (1987)
Noda, Y.; Takai, K.; Tokuyama, T.; Narumiya, S.; Ushiro, H.; Hayaishi, O.: Enzymatic oxidation of acetyltryptophanamide-and tryptophan-containing peptides. Formation of dehydrotryptophan. J. Biol. Chem., 252, 4413–4415 (1977)
Takai, K.; Sasai, Y.; Morimoto, H.; Yamazaki, H.; Yoshii, H.; Inoue, S.: Enzymatic dehydrogenation of tryptophan residues of human globins by tryptophan side chain oxidase II. J. Biol. Chem., 259, 4452–4457 (1984)
Takai, K.; Ushiro, H.; Noda, Y.; Narumiya, S.; Tokuyama, T.; Hayaishi, O.: cristalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives. J. Biol. Chem., 252, 2638–2656 (1977)
Narumiya, S.; Takai, K.; Tokuyama, T.; Noda, Y.; Ushiro, H.; Hayaishi, O.: A new metabolic pathway of tryptophan initiated by tryptophan side chain oxidase. J. Biol. Chem., 254, 7007–7015 (1979)
Roberts, J.; Rosenfeld, H.J.: Isolation, crystallization, and properties of indolyl-3-alkane α-hydroxylase. A novel tryptophan-metabolizing enzyme. J. Biol. Chem., 252, 2640–2647 (1977)
Zavala, F.; Takai, K.; Hayaishi, O.: Isolation and characterization of the common intermediate in dichotomous reaction catalyzed by tryptophan side chain oxidase. J. Biol. Chem., 258, 344–351 (1983)
Ito, S.; Takai, K.; Tokuyama, T.; Hayaishi, O.: Enzymatic modification of tryptophan residues by tryptophan side chain oxidase I and II from Pseudomonas. J. Biol. Chem., 256, 7834–7843 (1981)
Ushiro, H.; Takai, K.; Narumiya, S.; Ito, S.; Hayaishi, O.: Isolation and reconstitution of two electron transfer components of tryptophan side chain oxidase. J. Biol. Chem., 254, 11794–11797 (1979)
Ushiro, H.; Takai, K.; Noda, Y.; Narumiya, S.; Tokuyama, T.; Hayaishi, O.: Tryptophan side chain oxidase from Pseudomonas. Oxidation of skatole to indole-3-carboxaldehyde via indole-3-methanol. J. Biol. Chem., 253, 9002–9008 (1978)
Noda, Y.; Takai, K.; Tokuyama, T.; Narumiya, S.; Ushiro, H.; Hayaishi, O.: Tryptophan side chain oxidase from Pseudomonas. pH-Dependent formation of α, β-didehydro, β-hydroxy, and β-keto derivatives of N-acetyltryptophanamide. J. Biol. Chem., 253, 4819–4822 (1978)
Ho, D.H.; Covington, W.P.; Wallerstein, R.O.; Hester, J.P.; Lin, J.R.; Brown, N.S.; Newman, R.A.; Krakoff, I.H.; Freireich, E.J.: Depletion of patients’ plasma tryptophan using tryptophan side-chain oxidase columns. Cancer Invest., 11, 252–257 (1993)
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(2006). Tryptophan 2′-dioxygenase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37704-2_111
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DOI: https://doi.org/10.1007/3-540-37704-2_111
Publisher Name: Springer, Berlin, Heidelberg
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