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Tetrahydrobiopterin: biochemistry and pathophysiology
Open accessAbstract
BH4 (6R-L-erythro-5,6,7,8-tetrahydrobiopterin) is an essential cofactor of a set of enzymes that are of central metabolic importance, including four aromatic amino acid hydroxylases, alkylglycerol mono-oxygenase and three NOS (NO synthase) isoenzymes. Consequently, BH4 is present in probably every cell or tissue of higher organisms and plays a key role in a number of biological processes and pathological states associated with monoamine neurotransmitter formation, cardiovascular and endothelial dysfunction, the immune response and pain sensitivity. BH4 is formed de novo from GTP via a sequence of three enzymatic steps carried out by GTP cyclohydrolase I, 6-pyruvoyltetrahydropterin synthase and sepiapterin reductase. An alternative or salvage pathway involves dihydrofolate reductase and may play an essential role in peripheral tissues. Cofactor regeneration requires pterin-4a-carbinolamine dehydratase and dihydropteridine reductase, except for NOSs, in which the BH4 cofactor undergoes a one-electron redox cycle without the need for additional regeneration enzymes. With regard to the regulation of cofactor biosynthesis, the major controlling point is GTP cyclohydrolase I. BH4 biosynthesis is controlled in mammals by hormones and cytokines. BH4 deficiency due to autosomal recessive mutations in all enzymes, except for sepiapterin reductase, has been described as a cause of hyperphenylalaninaemia. A major contributor to vascular dysfunction associated with hypertension, ischaemic reperfusion injury, diabetes and others, appears to be an effect of oxidized BH4, which leads to an increased formation of oxygen-derived radicals instead of NO by decoupled NOS. Furthermore, several neurological diseases have been suggested to be a consequence of restricted cofactor availability, and oral cofactor replacement therapy to stabilize mutant phenylalanine hydroxylase in the BH4-responsive type of hyperphenylalaninaemia has an advantageous effect on pathological phenylalanine levels in patients.
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“In this case, the development of tolerance was mainly due to mitochondrial ROS release and was independent of NOX, whereas the activation of NOX, triggered by mitochondrial ROS, was the effector of the endothelial dysfunction associated to nitroglycerin tolerance (1004).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1004]
In the citing paper
“Through these enzymes, BH4 is required for nitric oxide (NO) production, metabolism of ether lipids, phenylalanine catabolism, and synthesis of the amine neurotransmitters norepinephrine, epinephrine, serotonin, and dopamine.”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Werner et al., 2011
In the citing paper
“GTP cyclohydrolase I (GCH1) is the rate-limiting enzyme for BH4 biosynthesis (Werner et al., 2011; Figure 4).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Werner et al., 2011
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Metadata
- Authors
- Werner, E. R., Blau, N., & Thöny, B.
- Affiliations
- Innsbruck Medical University (AT)
- University of Zurich (CH)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2011-08-26
- Volume
- 438
- Issue
- 3
- Pages
- 397-414
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2109852750
- Cited by
- 493
- References
- 228
- Citations by year
- 2026: 38 · 2025: 39 · 2024: 31 · 2023: 32 · 2022: 39 · 2021: 43 · 2020: 27 · 2019: 38 · 2018: 32 · 2017: 24 · 2016: 24 · 2015: 36 · 2014: 33 · 2013: 34 · 2012: 21
- FWCI
- 3.39
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- Austrian Science Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Folate and B Vitamins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- tetrahydrobiopterin, BH4 biosynthesis, GTP cyclohydrolase I, sepiapterin reductase, dihydrofolate reductase, dihydropteridine reductase, aromatic amino acid hydroxylases, nitric oxide synthase, hyperphenylalaninemia, phenylalanine hydroxylase, vascular dysfunction, hypertension, ischemia-reperfusion injury, diabetes mellitus, monoamines, endothelial dysfunction, immune response, pain sensitivity
- MeSH terms
- Animals, Biopterins, Humans, Hypertension, Phenylalanine, Phenylalanine Hydroxylase, Phenylketonurias, Nitric Oxide Synthase
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