The DOI matches its Crossref record.
Three-Dimensional Structure of Human Tryptophan Hydroxylase and Its Implications for the Biosynthesis of the Neurotransmitters Serotonin and Melatonin,
Abstract
Tryptophan hydroxylase oxidizes L-tryptophan to 5-hydroxy-L-tryptophan in the rate-determining step of serotonin biosynthesis. We have determined the X-ray crystal structure (1.7 A) of a truncated functional form of human tryptophan hydroxylase with the bound cofactor analogue 7,8-dihydro-L-biopterin, providing the first atomic-resolution information for the catalytic domain of this important enzyme. Comparison of the three-dimensional structures of all three members of the aromatic amino acid hydroxylase family--tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase--reveals important differences at the active sites.
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Citations
Cited by
Karve, T. M., & Cheema, A. K. (2011) · Journal of Amino Acids · doi:10.4061/2011/207691 · Cited by 364
Reinisalo, M., Kårlund, A., Koskela, A., Kaarniranta, K., & Karjalainen, R. O. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/340520 · Cited by 284
Mechanism of Aromatic Amino Acid Hydroxylation
Fitzpatrick, P. F. (2003) · Biochemistry · doi:10.1021/bi035656u · Cited by 278
Neural versus alternative integrative systems: molecular insights into origins of neurotransmitters
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
Metadata
- Authors
- Wang, L., Erlandsen, H., Haavik, J., Knappskog, P. M., & Stevens, R. C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-09-26
- Volume
- 41
- Issue
- 42
- Pages
- 12569-12574
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2027372708
- Cited by
- 178
- References
- 0
- FWCI
- 4.21
- Type
- journal article
- Language
- en
- Open access
- closed
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