EC Number   |
Subunits |
Reference |
|---|
    6.3.1.9 | ? |
x * 74500, recombinant detagged enzyme, SDS-PAGE |
-, 727114 |
| 6.3.1.9 | ? |
x * 79000, recombinant enzyme, SDS-PAGE |
-, 744964 |
| 6.3.1.9 | ? |
x * 82000, SDS-PAGE |
964 |
| 6.3.1.9 | monomer |
1 * 73560, deduced from nucleotide sequence |
652306 |
| 6.3.1.9 | monomer |
1 * 73744, MALDI mass spectrometry |
652306 |
| 6.3.1.9 | monomer |
1 * 74500, SDS-PAGE |
652306 |
| 6.3.1.9 | monomer |
1 * 87000, SDS-PAGE |
971 |
| 6.3.1.9 | More |
in vivo a complex between EC 6.3.1.8 and EC 6.3.1.9 exists that persists during purification |
964 |
| 6.3.1.9 | More |
secondary, tertiary, and domain structures, determined from three crystal forms, revealing two catalytic domains. The N-terminal domain, a cysteine, histidine-dependent amidohydrolase/peptidase amidase, is a papain-like cysteine protease, and the C-terminal synthetase domain displays an ATP-grasp family fold common to C:N ligases |
693074 |
