EC 3.6.1.67 - Dihydroneopterin triphosphate diphosphatase

  IntEnz view ENZYME view
XML

IntEnz Enzyme Nomenclature
EC 3.6.1.67

Names

Accepted name:
dihydroneopterin triphosphate diphosphatase
Other names:
dihydroneopterin triphosphate pyrophosphohydrolase
NUDT1 (gene name)
folQ (gene name)
nudB (gene name)
Systematic name:
7,8-dihydroneopterin 3'-triphosphate diphosphohydrolase

Reaction

Cofactor

Comments:

Requires Mg2+. The enzyme participates in a folate biosynthesis pathway, which is found in bacteria, fungi, and plants.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Suzuki, Y., Brown, G. M.
    The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase.
    J. Biol. Chem. 249 : 2405-2410 (1974). [PMID: 4362677]
  2. O'Handley, S. F., Frick, D. N., Bullions, L. C., Mildvan, A. S., 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 : 24649-24654 (1996). [PMID: 8798731]
  3. Klaus, S. M., Wegkamp, A., Sybesma, W., Hugenholtz, J., Gregory, J. F., Hanson, A. D.
    A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants.
    J. Biol. Chem. 280 : 5274-5280 (2005). [PMID: 15611104]
  4. Gabelli, S. B., Bianchet, M. A., Xu, W., Dunn, C. A., Niu, Z. D., Amzel, L. M., Bessman, M. J.
    Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.
    Structure 15 : 1014-1022 (2007). [PMID: 17698004]

[EC 3.6.1.67 created 2014]