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Product membrane-bound ATP synthase, F1 sector, alpha-subunit
| membrane-bound ATP synthase, F1 sector, alpha-subunit |
| F1-ATPase, alpha-subunit |
| F1F0-type proton-ATPase/ATP synthase, alpha-subunit |
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- Weber, J., C. Bowman, S. Wilke-Mounts, A.E. Senior 1995. alpha-Aspartate 261 is a key residue in noncatalytic sites of Escherichia coli F1-ATPase. J.Biol.Chem. 270:21045-0
- Hatch, L.P., G.B. Cox, S.M. Howitt 1995. The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity. J.Biol.Chem. 270:29407-0
- Moritani, C., K. Sawada, K. Takemoto, Y. Shin, S. Nemoto, T. Noumi, H. Kanazawa 1996. Interactions of the F1-ATPase subunits from Escherichia coli detected by the yeast two-hybrid system. Biochim.Biophys.Acta 1274:67-72
- Weber, J., A.E. Senior 1996. Binding and hydrolysis of TNP-ATP by Escherichia coli F1-ATPase. J.Biol.Chem. 271:3474-3477
- Le, N.P., H. Omote, Y. Wada, M.K. Al-Shawi, R.K. Nakamoto, M. Futai 2000. Escherichia coli ATP synthase alpha subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to the st