Enzyme

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EC Tree
     3. Hydrolases
        3.6 Acting on acid anhydrides
            3.6.1 In phosphorus-containing anhydrides
ID:3.6.1.67
Description:Dihydroneopterin triphosphate diphosphatase.
Alternative Name: Dihydroneopterin triphosphate pyrophosphohydrolase.
Cath: 3.90.79.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.6.1.67
BRENDA Enzyme Link: BRENDA 3.6.1.67
KEGG Enzyme Link: KEGG3.6.1.67
BioCyc Enzyme Link: BioCyc 3.6.1.67
ExPASy Enzyme Link: ExPASy3.6.1.67
EC2PDB Enzyme Link: EC2PDB 3.6.1.67
ExplorEnz Enzyme Link: ExplorEnz 3.6.1.67
PRIAM enzyme-specific profiles Link: PRIAM 3.6.1.67
IntEnz Enzyme Link: IntEnz 3.6.1.67
MEDLINE Enzyme Link: MEDLINE 3.6.1.67
MSA:

3.6.1.67;

Phylogenetic Tree:

3.6.1.67;

Uniprot:
M-CSA:
RHEA:25302 7,8-dihydroneopterin 3'-triphosphate + H2O = 7,8-dihydroneopterin 3'-phosphate + diphosphate + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme.O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ1996 Oct 48798731
The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase.Suzuki Y, Brown GM1974 Apr 254362677
Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis.Gabelli SB, Bianchet MA, Xu W, Dunn CA, Niu ZD, Amzel LM, Bessman MJ2007 Aug17698004
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants.Klaus SM, Wegkamp A, Sybesma W, Hugenholtz J, Gregory JF 3rd, Hanson AD2005 Feb 1815611104