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Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases.
Open accessAbstract
A full-length cDNA for tryptophan hydroxylase was cloned from rabbit pineal body by screening an expression library with antibody against rat phenylalanine hydroxylase, which crossreacts with rabbit tryptophan hydroxylase. Clones producing immunoreactive material contain sequences homologous to, yet distinct from, phenylalanine hydroxylase. The rabbit cDNA hybridizes to mRNA in pineal body and brainstem but not in liver. Comparison of the rabbit tryptophan hydroxylase sequence with the sequences of phenylalanine hydroxylase and tyrosine hydroxylase demonstrates that these three biopterin-dependent aromatic amino acid hydroxylases are highly homologous, reflecting a common evolutionary origin from a single primordial genetic locus. The pattern of sequence homology supports the hypothesis that the carboxyl-terminal two-thirds of the molecules constitute the enzymatic activity cores, and the amino-terminal thirds of the molecules constitute domains for substrate specificity.
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Cited by
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Moroz, L. L., Romanova, D. Y., & Kohn, A. B. (2021) · Philosophical Transactions of the Royal Society B · doi:10.1098/rstb.2019.0762 · Cited by 130
Complex molecular regulation of tyrosine hydroxylase
Tekin, I., Roskoski, R., Carkaci-Salli, N., & Vrana, K. E. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1238-7 · Cited by 128
Døskeland, A. P., & Flatmark, T. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02808.x · Cited by 53
Metadata
- Authors
- Grenett, H. E., Ledley, F. D., Reed, L. L., & Woo, S. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1987-08
- Volume
- 84
- Issue
- 16
- Pages
- 5530-5534
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2067043949
- Cited by
- 183
- References
- 0
- FWCI
- 7.04
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases. https://app.cochat.ai/papers/10.1073/pnas.84.16.5530
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- Grenett, H. E., Ledley, F. D., Reed, L. L., & Woo, S. L. (1987). Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.84.16.5530
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