H+-exporting ATPase

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In enzymology, a H+-exporting ATPase (EC 3.6.3.6) is an enzyme that catalyzes the chemical reaction

ATP + H₂O + H⁺in $\rightleftharpoons$ ADP + phosphate + H⁺out

The 3 substrates of this enzyme are ATP, H₂O, and H⁺, whereas its 3 products are ADP, phosphate, and H⁺.

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (H+-exporting). Other names in common use include proton-translocating ATPase, yeast plasma membrane H+-ATPase, yeast plasma membrane ATPase, and ATP phosphohydrolase. This enzyme participates in oxidative phosphorylation. It employs one cofactor, H+.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1MHS.

[edit] References

IUBMB entry for 3.6.3.6
BRENDA references for 3.6.3.6 (Recommended.)
PubMed references for 3.6.3.6
PubMed Central references for 3.6.3.6
Google Scholar references for 3.6.3.6
Goffeau A, Slayman CW (1981). "The proton-translocating ATPase of the fungal plasma membrane". Biochim. Biophys. Acta. 639: 197–223. PMID 6461354.
Serrano R, Kielland-Brandt MC, Fink GR (1986). "Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases". Nature. 319: 689–93. doi:10.1038/319689a0. PMID 3005867.
Serrano R, Portillo F (1990). "Catalytic and regulatory sites of yeast plasma membrane H(+)-ATPase studied by directed mutagenesis". Biochim. Biophys. Acta. 1018: 195–9. PMID 2144186.