Folate synthesis: an old enzyme identified.
In this issue of Structure, Amzel, Bessman, and colleagues (Gabelli et al., 2007) present the crystal structure of a 17 kDa Nudix hydrolase from Escherichia coli previously characterized as a dATPase and provide evidence that it functions in vivo to remove pyrophosphate from the folate precursor dihydroneopterin triphosphate.
McLennan
Alexander G
AG
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005492:Folic Acid / Q000096:biosynthesis*; D008969:Molecular Sequence Data; D019798:Neopterin / Q000031:analogs & derivatives / Q000096:biosynthesis / Q000378:metabolism; D011755:Pyrophosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction; D000096964:Nudix Hydrolases
D005492:Folic Acid; D019798:Neopterin; D011755:Pyrophosphatases; D000096964:Nudix Hydrolases; C013490:dihydroneopterin triphosphate