CATH Classification

Domain Context

CATH Clusters

Superfamily Nucleoside Triphosphate Pyrophosphohydrolase
Functional Family diphosphoinositol polyphosphate phosphohydrolase 1

Enzyme Information

3.6.1.52
Diphosphoinositol-polyphosphate diphosphatase.
based on mapping to UniProt Q8NFP7
Diphospho-myo-inositol polyphosphate + H(2)O = myo-inositol polyphosphate + phosphate.
-!- This enzyme hydrolyzes the diphosphate bond, leaving a phospho group where a diphospho group had been. -!- It can also act on bis(adenosine) diphosphate.
3.6.1.60
Diadenosine hexaphosphate hydrolase (AMP-forming).
based on mapping to UniProt Q8NFP7
(1) P(1),P(6)-bis(5'-adenosyl)hexaphosphate + H(2)O = adenosine 5'-pentaphosphate + AMP. (2) P(1),P(5)-bis(5'-adenosyl)pentaphosphate + H(2)O = adenosine 5'-tetraphosphate + AMP.
-!- A divalent cation is essential for activity. -!- Mn(2+) (2-6 mM) is most effective. -!- The enzyme controls intracellular levels of P(1),P(5)- bis(5'-adenosyl)pentaphosphate and P(1),P(6)- bis(5'-adenosyl)hexaphosphate. -!- Weak activity with P(1),P(4)-bis(5'-adenosyl)tetraphosphate. -!- Marked preference for adenine over guanine nucleotides.

UniProtKB Entries (1)

Q8NFP7
NUD10_HUMAN
Homo sapiens
Diphosphoinositol polyphosphate phosphohydrolase 3-alpha

PDB Structure

PDB 3MCF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of human diphosphoinositol polyphosphate phosphohydrolase 3-alpha
Tresaugues, L., Welin, M., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, I., Karlberg, T., Kol, S., Kotenyova, T., Moche, M., Nyman, T., Persson, C., Schuler, H., Schutz, P., Siponen, M.I., Thorsell, A.G., van der Berg, S., Wahlberg, E., Weigelt, J., Wisniewska, M., Nordlund, P.
To be Published