Tetrahydrobiopterin Binding to Aromatic Amino Acid Hydroxylases. Ligand Recognition and Specificity
✍ Scribed by Teigen, Knut; Dao, Khanh K.; McKinney, Jeffrey A.; Gorren, Antonius C. F.; Mayer, Bernd; Frøystein, Nils Åge; Haavik, Jan; Martínez, Aurora
- Book ID
- 127070464
- Publisher
- American Chemical Society
- Year
- 2004
- Tongue
- English
- Weight
- 727 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0022-2623
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Tetrahydrobiopterin (BH4) levels and GTP cyclohydrolase activity (GTP-CH) were measured in tissues from mutants and controls of 24 different mouse strains to identify mutants that might be suitable models for diseases which are characterized by a deficiency of the biopterin cofactor, such as parkins
## Abstract The biosynthesis of serotonin requires aromatic substrates to be bound in the active sites of the enzymes tryptophan hydroxylase and aromatic amino acid decarboxylase. These aromatic substrates are held in place partially by dispersion and induction interactions with the enzymes' aromat