Abstract
Escherichia coli ATP synthase (H+-ATPase) is the first energy transducing enzyme whose primary structure has been determined from the DNA sequence of the cloned genes (unc operon) (Kanazawa and Futai, 1982; Futai and Kanazawa, 1983; Walker et al., 1984; Senior, 1985). This enzyme (F0F1) is similar to those found in mitochondria or chloroplasts and the catalytic entity F1 (F1-ATPase) consists of five subunits α, β, γ, δ and ε. Studies of E. coli F1 are advantageous because variant (mutant) enzymes with defined amino acid substitutions can be easily obtained. Studies on such enzymes may help to understand mechanism and assembly of the normal enzyme. Furthermore most of the results can be extended to the eukaryotic enzymes. This short article summarizes our recent results on the genetic studies of F1-ATPase.
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© 1989 Plenum Press, New York
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Futai, M., Noumi, T., Maeda, M. (1989). Genetic Studies of F1-ATPase of Escherichia Coli . In: Marzuki, S. (eds) Molecular Structure, Function, and Assembly of the ATP Synthases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0593-4_2
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DOI: https://doi.org/10.1007/978-1-4613-0593-4_2
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