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Feedback Regulation Mechanisms for the Control of GTP Cyclohydrolase I Activity
Abstract
Guanosine triphosphate (GTP) cyclohydrolase I, the rate-limiting enzyme in the biosynthesis of tetrahydrobiopterin (BH 4 ), is subject to feedback inhibition by BH 4 , a cofactor for phenylalanine hydroxylase. Inhibition was found to depend specifically on BH 4 and the presence of another protein (p35). The inhibition occurred through BH 4 -dependent complex formation between p35 protein and GTP cyclohydrolase I. Furthermore, the inhibition was specifically reversed by phenylalanine, and, in conjunction with p35, phenylalanine reduced the cooperativity of GTP cyclohydrolase I. These findings also provide a molecular basis for high plasma BH 4 concentrations observed in patients with hyperphenylalaninemia caused by phenylalanine hydroxylase deficiency.
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Cited by
GTP Cyclohydrolase 1/Tetrahydrobiopterin Counteract Ferroptosis through Lipid Remodeling
Kraft, V. A. N., Bezjian, C. T., Pfeiffer, S., Ringelstetter, L., Müller, C., Zandkarimi, F., Merl-Pham, J., Bao, X., Anastasov, N., Kössl, J., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.9b01063 · Cited by 1,298
Conn, M. M., & Rebek, J. (1997) · Chemical Reviews · doi:10.1021/cr9603800 · Cited by 1,075
Tetrahydrobiopterin biosynthesis, regeneration and functions
Thöny, B., Auerbach, G., & Blau, N. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3470001 · Cited by 893
Ichinose, H., Ohye, T., Takahashi, E.-I., Seki, N., Hori, T.-A., Segawa, M., Nomura, Y., Endo, K., Tanaka, H., Tsuji, S., et al. (1994) · Nature Genetics · doi:10.1038/ng1194-236 · Cited by 771
Kolluru, G. K., Bir, S. C., & Kevil, C. G. (2012) · International Journal of Vascular Medicine · doi:10.1155/2012/918267 · Cited by 720
Metadata
- Authors
- Harada, T., Kagamiyama, H., & Hatakeyama, K.
- Venue
- Science
- Published
- 1993-06-04
- Volume
- 260
- Issue
- 5113
- Pages
- 1507-1510
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2051380872
- Cited by
- 162
- References
- 0
- FWCI
- 5.50
- Type
- journal article
- Language
- en
- Open access
- closed
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