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Partial Purification and Characterization of Tryptophan Hydroxylase from Rabbit Hindbrain
Open accessAbstract
With the use of a rapid, sensitive fluorometric assay, tryptophan hydroxylase from rabbit hindbrain has been partially purified. The enzyme resembles phenylalanine and tyrosine hydroxylases in many respects. For example, the hydroxylation reaction shows an absolute requirement for a tetrahydropterin and is stimulated by reduced pyridine nucleotide, dihydropteridine reductase, and catalase. Fe2+ also stimulates the reaction but only in the absence of catalase; this finding suggests that catalase or Fe2+ protects a sensitive component of the tryptophan hydroxylation system from inactivation by H2O2. Just as with the other pterin-dependent aromatic amino acid hydroxylases, the apparent Km of tryptophan hydroxylase for its amino acid substrate and for oxygen are markedly lower in the presence of tetrahydrobiopterin than they are in the presence of the cofactor analogue, dimethyltetrahydropterin. In addition, high concentrations of tryptophan inhibit the reaction in the presence of tetrahydrobiopterin, but not in the presence of the dimethylpterin. The stoichiometry of the reaction catalyzed by tryptophan hydroxylase in the presence of tetrahydrobiopterin has been determined.
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Citations
Cited by
Effect of anoxia on ion distribution in the brain
Hansen, A. J. (1985) · Physiological Reviews · doi:10.1152/physrev.1985.65.1.101 · Cited by 1,346
Reduced Biopterin as a Cofactor in the Generation of Nitrogen Oxides by Murine Macrophages
Kwon, N. S., Nathan, C. F., & Stuehr, D. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47089-0 · Cited by 570
Tryptophan metabolism in the central nervous system: medical implications
Ruddick, J. P., Evans, A. K., Nutt, D. J., Lightman, S. L., Rook, G. A. W., & Lowry, C. A. (2006) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399406000068 · Cited by 519
Physiopharmacological interactions between stress hormones and central serotonergic systems
Chaouloff, F. (1993) · Brain Research Reviews · doi:10.1016/0165-0173(93)90005-k · Cited by 493
The biological significance of substrate inhibition: A mechanism with diverse functions
Reed, M. C., Lieb, A., & Nijhout, H. F. (2010) · BioEssays · doi:10.1002/bies.200900167 · Cited by 335
Metadata
- Authors
- Friedman, P. A., Kappelman, A. H., & Kaufman, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1972-07
- Volume
- 247
- Issue
- 13
- Pages
- 4165-4173
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1571821264
- Cited by
- 445
- References
- 0
- FWCI
- 14.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Friedman, P. A., Kappelman, A. H., & Kaufman, S. (1972). Partial Purification and Characterization of Tryptophan Hydroxylase from Rabbit Hindbrain. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)45055-2
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