TABLE 8.
Comparison of basic properties of ATPases from methanogenic archaeaa
| Organism | No. of polypeptides (kDa) | No. of identified genes | Coupling ion | Inhibitors | Molecular mass of proteolipid (kDa) | Reference |
|---|---|---|---|---|---|---|
| M. barkeri | 2–6 (420) | 2 | H+ | DCCD, NO3− | 6 | 244 |
| M. thermophila | 5 (540) | ND | H+ | DCCD, NO3− | (?) | 242 |
| M. tindarius | 4 (445) | ND | H+ | DCCD, NO3− | 5.5 | 481 |
| M. mazei | 6 | 10 | H+ | DCCD, NO3− | 7 | 602 |
| M. thermoautotrophicum | 9–10b | H+ | NR | 15.6b | 290 | |
| M. jannaschii | 9–10b | ? | ? | 21.3 | 87 | |
| M. voltae | 3 | NA+ (?) | DCCD, NO3− | ND | 96 |
a
Compared to that for Sulfolobus and Halobacterium, knowledge of the catalytic properties is still rudimentary. Inhibitory function of DCCD refers to the membrane-bound ATPase activities. ND, not determined; NR, not reported.
b
Data extracted from genome sequences.