TABLE 2.
Relative specificities of Nudix hydrolases
| Substrated | Relative specificitya (%) of:
|
||||
|---|---|---|---|---|---|
| PnhA | YgdPc | IalAc | InvAc | NudAc | |
| Ap5A | 100b | 100 | 77 | 100 | 34 |
| Ap6A | 43.5 | 92 | 67 | 66 | 45 |
| Ap4A | 13.5 | 14 | 100 | 5 | 100 |
| Ap3A | <1 | <1 | <1 | <1 | 7 |
| GDP-mannose | <0.5 | <1 | <1 | <1 | <1 |
| ADP-ribose | <0.5 | <1 | <1 | 4 | 0 |
| UDP-glucose | <0.5 | NDe | <1 | ND | ND |
| NADH | <0.5 | <1 | <1 | <1 | 0 |
| FAD | <0.5 | ND | ND | ND | ND |
a
Relative specificities were expressed as the percentage of activity of each enzyme, with the preferred substrate set at 100.
b
Substrates were present at a concentration of 1 mM or 2 mM in the standard assay.
c
The data for E. coli YgdP, B. bacilliformis IalA, R. prowazekii InvA, and H. pylori NudA were taken from references 7, 16, 24, and 34, respectively, and included for comparison.
d
Ap5A, adenosine (5′)-pentaphospho-(5′)-adenosine; Ap6A, adenosine (5′)-hexaphospho-(5′)-adenosine, Ap4A, adenosine (5′)-tetraphospho-(5′)-adenosine; Ap3A, adenosine (5′)-triphospho-(5′)-adenosine.
e
ND, not determined.