The Enzyme Database

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EC 7.1.2.2     
Accepted name: H+-transporting two-sector ATPase
Reaction: ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
Glossary: In Fo, the "o" refers to oligomycin. F0 is incorrect
Other name(s): ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (Fo F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase
Systematic name: ATP phosphohydrolase (two-sector, H+-transporting)
Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9–12 c subunits rotate by consecutive 120° angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53–61. [PMID: 2425739]
2.  Boyer, P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215–250. [DOI] [PMID: 8417777]
3.  Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621–628. [DOI] [PMID: 8065448]
4.  Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr. Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria. Microbiology 142 (1996) 17–32. [DOI] [PMID: 8581162]
5.  Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299–302. [DOI] [PMID: 9069291]
6.  Turina, P., Samoray, D. and Graber, P. H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes. EMBO J. 22 (2003) 418–426. [PMID: 12554643]
[EC 7.1.2.2 created 1984 as EC 3.6.1.34, transferred 2000 to EC 3.6.3.14, transferred 2018 to EC 7.1.2.2]
 
 


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