EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages  |
Year |
Organism |
PubMed ID |
|---|
    3.6.1.67 | 758154 |
Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase New clues into catalytic mechanism |
PLoS ONE |
12 |
e0180241 |
2017 |
Escherichia coli |
28742822 |
| 3.6.1.67 | 728808 |
Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis |
Structure |
15 |
1014-1022 |
2007 |
Escherichia coli |
17698004 |
| 3.6.1.67 | 727800 |
The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase |
J. Biol. Chem. |
249 |
2405-2410 |
1974 |
Escherichia coli |
4362677 |
| 3.6.1.67 | 729956 |
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 |
Escherichia coli |
8798731 |
| 3.6.1.67 | 727354 |
Dual hydrolysis of diphosphate and triphosphate derivatives of oxidized deoxyadenosine by Orf17 (NtpA), a MutT-type enzyme |
DNA Repair |
4 |
33-39 |
2005 |
Escherichia coli |
15533835 |
| 3.6.1.67 | 727852 |
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants |
J. Biol. Chem. |
280 |
5274-5280 |
2004 |
Lactococcus lactis |
15611104 |
| 3.6.1.67 | 727852 |
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants |
J. Biol. Chem. |
280 |
5274-5280 |
2004 |
Arabidopsis thaliana |
15611104 |
| 3.6.1.67 | 727852 |
A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants |
J. Biol. Chem. |
280 |
5274-5280 |
2004 |
Lactococcus lactis NZ9000 |
15611104 |
