ExplorEnz: EC 3.6.1.67

Your query returned 1 entry. Printable version

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, Gene, KEGG, MetaCyc, PDB

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. [DOI] [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. [DOI] [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. [DOI] [PMID: 17698004]

[EC 3.6.1.67 created 2014]