EC Number   |
Title |
Organism |
|---|
    3.6.1.67 | Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase New clues into catalytic mechanism |
Escherichia coli |
| 3.6.1.67 | A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants |
Lactococcus lactis |
| 3.6.1.67 | A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants |
Arabidopsis thaliana |
| 3.6.1.67 | A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants |
Lactococcus lactis NZ9000 |
| 3.6.1.67 | Dual hydrolysis of diphosphate and triphosphate derivatives of oxidized deoxyadenosine by Orf17 (NtpA), a MutT-type enzyme |
Escherichia coli |
| 3.6.1.67 | Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme |
Escherichia coli |
| 3.6.1.67 | Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis |
Escherichia coli |
| 3.6.1.67 | The biosynthesis of folic acid. XII. Purification and properties of dihydroneopterin triphosphate pyrophosphohydrolase |
Escherichia coli |
