EC Number   |
Subunits |
Reference |
|---|
    3.5.4.10 | ? |
open reading frame of 527 amino acids, complementatition analysis show that the IMP cyclohydrolase activity resides on the N-terminal region |
172168 |
| 3.5.4.10 | ? |
predicted size 57335, 52% identical to B. subtilis sequence |
172169 |
| 3.5.4.10 | ? |
x * 21500, SDS-PAGE |
651694 |
| 3.5.4.10 | ? |
x * 22000, recombinant enzyme, SDS-PAGE |
685152 |
| 3.5.4.10 | ? |
x * 22000, SDS-PAGE |
-, 757625 |
| 3.5.4.10 | dimer |
2 * 54000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking studies, the purified recombinant enzyme and its truncated domains exist mainly in dimeric form |
756701 |
| 3.5.4.10 | dimer |
2 * 55746, open reading frame |
1259 |
| 3.5.4.10 | dimer |
2 * 62100, protein mobility assay |
172161 |
| 3.5.4.10 | dimer |
2 * 64200, open reading frame, polypeptide of 592 amino acids, 91% similar to human IMPCHase |
172164 |
| 3.5.4.10 | dimer |
2 * 64422, open reading frame, gel filtration |
172160 |
