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J Biol Chem, Vol. 273, Issue 43, 28132-28141, October 23, 1998

Biosynthesis of Pteridines
NMR STUDIES ON THE REACTION MECHANISMS OF GTP CYCLOHYDROLASE I, PYRUVOYLTETRAHYDROPTERIN SYNTHASE, AND SEPIAPTERIN REDUCTASE

From the Institut für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstrasse 4, D-85747 Garching, Federal Republic of Germany

GTP cyclohydrolase I catalyzes a ring expansion affording dihydroneopterin triphosphate from GTP. [1',2',3',4',5'-¹³C₅,2'-²H₁]GTP was prepared enzymatically from [U-¹³C₆]glucose for use as enzyme substrate. Multinuclear NMR experiments showed that the reaction catalyzed by GTP cyclohydrolase I involves the release of a proton from C-2' of GTP that is exchanged with the bulk solvent. Subsequently, a proton is reintroduced stereospecifically from the bulk solvent. This is in line with an Amadori rearrangement mechanism. The proton introduced from solvent occupies the pro-7R position in the enzyme product. The data also confirm that the reaction catalyzed by pyruvoyltetrahydropterin synthase results in the incorporation of solvent protons into positions C-6 and C-3' of the enzyme product. On the other hand, the reaction catalyzed by sepiapterin reductase does not involve any detectable incorporation of solvent protons into tetrahydrobiopterin.

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