Abstract
GTP cyclohydrolase I (GTPCH) is the first and rate-limiting enzyme in the tetrahydrobiopterin (BH4) biosynthetic pathway. BH4 is the essential cofactor for the pterin-dependent monooxygenases which include tyrosine and tryptophan hydroxylase, enzymes that are rate limiting in the biosynthesis of catecholamines and indolamines. BH4 is also required as a cofactor for the family of nitric oxide synthases1,2. We have obtained a clone for GTPCH based on the recently published full-length cDNA encoding GTPCH from rat liver3,4. The in situ hybridization technique was used to study the cellular localization and the relative levels of expression of GTPCH mRNA in the rat brain.
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Lentz, S.I., Hirayama, K., Kapatos, G. (1993). Localization of GTP Cyclohydrolase I (GTPCH) mRNA in the Rat Brain by in Situ Hybridization. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_33
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DOI: https://doi.org/10.1007/978-1-4615-2960-6_33
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