The Enzyme Database

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EC 3.6.1.67     
Accepted name: dihydroneopterin triphosphate diphosphatase
Reaction: 7,8-dihydroneopterin 3′-triphosphate + H2O = 7,8-dihydroneopterin 3′-phosphate + diphosphate
Other name(s): folQ (gene name); nudB (gene name); NUDT1 (gene name); dihydroneopterin triphosphate pyrophosphohydrolase
Systematic name: 7,8-dihydroneopterin 3′-triphosphate diphosphohydrolase
Comments: The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants. Requires Mg2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Suzuki, Y. and Brown, G.M. The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase. J. Biol. Chem. 249 (1974) 2405–2410. [PMID: 4362677]
2.  O'Handley, S.F., Frick, D.N., Bullions, L.C., Mildvan, A.S. and Bessman, M.J. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. J. Biol. Chem. 271 (1996) 24649–24654. [PMID: 8798731]
3.  Klaus, S.M., Wegkamp, A., Sybesma, W., Hugenholtz, J., Gregory, J.F., 3rd and Hanson, A.D. A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants. J. Biol. Chem. 280 (2005) 5274–5280. [PMID: 15611104]
4.  Gabelli, S.B., Bianchet, M.A., Xu, W., Dunn, C.A., Niu, Z.D., Amzel, L.M. and Bessman, M.J. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure 15 (2007) 1014–1022. [PMID: 17698004]
[EC 3.6.1.67 created 2014]
 
 


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