Abstract
GTP cyclohydrolase I of Escherichia coli converts [β,γ-methylene]GTP to a fluorescent product that is characterized as [β,γ-methylene]dihydroneopterin triphosphate. Interaction between the GTP analog and the enzyme gave a K i of 3.0 μ m, which may be compared to the K m of 0.1 μ m for GTP. This new analog of dihydroneopterin triphosphate may, in turn, be converted to the same greenish-yellow pteridines (compounds X, X1, and X2) that are obtained from dihydroneopterin triphosphate. Because of its stability to phosphatase action, this analog may be useful for studies in pteridine metabolism.
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