PMID:10378270
| Citation |
Ploom, T, Haussmann, C, Hof, P, Steinbacher, S, Bacher, A, Richardson, J and Huber, R (1999) Crystal structure of 7,8-dihydroneopterin triphosphate epimerase. Structure 7:509-16 |
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| Abstract |
Dihydroneopterin triphosphate (H2NTP) is the central substrate in the biosynthesis of folate and tetrahydrobiopterin. Folate serves as a cofactor in amino acid and purine biosynthesis and tetrahydrobiopterin is used as a cofactor in amino acid hydroxylation and nitric oxide synthesis. In bacteria, H2NTP enters the folate biosynthetic pathway after nonenzymatic dephosphorylation; in vertebrates, H2NTP is used to synthesize tetrahydrobiopterin. The dihydroneopterin triphosphate epimerase of Escherichia coli catalyzes the inversion of carbon 2' of H2NTP. |
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| Keywords |
Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Racemases and Epimerases/chemistry; Racemases and Epimerases/metabolism; Sequence Homology, Amino Acid |
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