Abstract
Pterins are very similar to flavins, and the reactions catalyzed by pterin monooxygenases (for a review, see Massey and Hemmerich, 1975) are very similar to those catalyzed by the flavin monooxygenases.
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References
Brenneman, A. R., and Kaufman, S., 1964. The role of tetrahydropterins in the enzymatic conversion of tyrosine to 3, 4-dihydroxyphenylalanine, Biochem. Biophys. Res. Commun.17: 177–183.
Daly, J., and Guroff, G., 1968. Production of m-methyltyrosine and p-hydroxyphenylalanine from o-methylphenylalanine by phenylalanine hydroxylase, Arch. Biochem. Biophys.125: 136–141.
Ellenbogen, L., Taylor, R. J., Jr., and Brundage, G. B., 1965. On the role of pteridines as cofactors for tyrosine hydroxylase, Biochem. Biophys. Res. Commun.19: 708–715.
Fisher, D. B., and Kaufman, S., 1973. Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase, J. Biol. Chem.248: 4300–4304.
Fisher, D. B., Kirkwood, R., and Kaufman, S., 1972. Rat liver phenylalanine hydroxylase, an iron enzyme, J. Biol. Chem.247: 5161–5167.
Guroff, G., Reifsnyder, C. A., and Daly, J., 1966a. Retention of deuterium in p-tryosine formed enzymatically from p-deuterophenylalanine, Biochem. Biophys, Res. Commun.24: 720–724.
Guroff, G., Kondo, K., and Daly, J., 1966b. The production of metachlorotyrosine from parachlorotyrosine by phenylalanine hydroxylase, Biochem. Biophys. Res. Commun.25: 623–628.
Guroff, G., Levitt, M., Daly, J., and Udenfriend, S., 1966c. The production of meta-tritiotyrosine from p-tritiophenylalanine by phenylalanine hydroxylase, Biochem. Biophys. Res. Commun.25: 253–259.
Guroff, G., Daly, J. W., Jerina, D. M., Renson, J., Witkop, B., and Udenfriend, S., 1967. Hydroxylation induced migration: The NIH shift, Science157: 1524–1530.
Jerina, D., Daly, J., Landis, W., Witkop, B., and Udenfriend, S., 1967. Intramolecular migration of deuterium during nonenzymic aromatic hydroxylation, J. Am. Chem. Soc.89: 3347–3349.
Kaufman, S., 1961. The enzymatic conversion of 4-fluorophenylalanine to tyrosine, Biochem. Biophys. Acta51: 619–621.
Kaufman, S., and Fisher, D. R., 1970. Purification and some physical properties of phenylalanine hydroxylase from rat liver, J. Biol. Chem.245: 4745–4750.
Kaufman, S., Bridgers, W. F., Eisenberg, F., and Friedman, S., 1962. The source of oxygen in the phenylalanine hydroxylase and the dopamine (3-hydroxylase catalyzed reactions, Biochem. Biophys. Res. Commun.9: 497–502.
Massey, V., and Hemmerich, P., 1975. Flavin and pteridine monooxygenases, in The Enzymes, Vol. 12, P. D. Boyer (ed.), Academic Press, New York, pp. 191–252.
Nagatsu, T., Levitt, M., and Udenfriend, S., 1964. Tyrosine hydroxylase: The initial step in norepinephrine biosynthesis, J. Biol. Chem.239: 2910–2917.
Renson, J., Daly, J., Weisbach, H., Witkop, B., and Udenfriend, S., 1966. Enzymatic conversion of 5-nitrotryptophan to 4-tritio-5-hydroxytryptophan, Biochem. Biophys. Res. Commun.25: 504–513.
Udenfriend, S., Zaltzman-Nireberg, P., Daly, J., Guroff, G., Chidsey, C., and Witkop, B., 1967. Intramolecular migration of deuterium and tritium during enzymatic hydroxylation of p-deuteroacetanilide and p-tritioacetanilide, Arch. Biochem. Biophys.120: 413–419.
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© 1985 Plenum Press, New York
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Ingraham, L.L., Meyer, D.L. (1985). Pterin Monooxygenases. In: Biochemistry of Dioxygen. Biochemistry of the Elements, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2475-1_13
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DOI: https://doi.org/10.1007/978-1-4613-2475-1_13
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