Abstract
GTP cyclohydrolase I catalyzes a ring expansion affording dihydroneopterin triphosphate from GTP (1, 2). The reaction involves the release of C-8 of GTP as formate. The catalytic domain of the human enzyme shows 37% identity with that of Escherichia coli. Both enzymes are toroid-shaped homodecamers with d5 symmetry and were recently shown to contain a catalytically essential zinc ion at each of the 10 equivalent active sites (Figure 1) (3, 4).
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Schramek, N. et al. (2002). Studies on the Reaction Mechanism of GTP Cyclohydrolase I. In: Milstien, S., Kapatos, G., Levine, R.A., Shane, B. (eds) Chemistry and Biology of Pteridines and Folates. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0945-5_28
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DOI: https://doi.org/10.1007/978-1-4615-0945-5_28
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