ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca2+ + Mg2+)-ATPase, HCO3−-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion[1][2][3][4][5][6] or the inverse reaction. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur. This process is widely used in all known forms of life.
Some such enzymes are integral membrane proteins (anchored within biological membranes), and move solutes across the membrane, typically against their concentration gradient. These are called transmembrane ATPases.
^Geider K, Hoffmann-Berling H (1981). "Proteins controlling the helical structure of DNA". Annual Review of Biochemistry. 50: 233–60. doi:10.1146/annurev.bi.50.070181.001313. PMID 6267987.
^Kielley WW (1961). "Myosin adenosine triphosphatase". In Boyer PD, Lardy H, Myrbäck K (eds.). The Enzymes. Vol. 5 (2nd ed.). New York: Academic Press. pp. 159–168.
^Martin SS, Senior AE (November 1980). "Membrane adenosine triphosphatase activities in rat pancreas". Biochimica et Biophysica Acta (BBA) - Biomembranes. 602 (2): 401–18. doi:10.1016/0005-2736(80)90320-x. PMID 6252965.
^Njus D, Knoth J, Zallakian M (1981). "Proton-linked transport in chromaffin granules". Current Topics in Bioenergetics. 11: 107–147. doi:10.1016/B978-0-12-152511-8.50010-4.
^Riley MV, Peters MI (June 1981). "The localization of the anion-sensitive ATPase activity in corneal endothelium". Biochimica et Biophysica Acta (BBA) - Biomembranes. 644 (2): 251–6. doi:10.1016/0005-2736(81)90382-5. PMID 6114746.
^Tjian R (1981). "Regulation of viral transcription and DNA replication by the SV40 large T antigen". Current Topics in Microbiology and Immunology. 93: 5–24. doi:10.1007/978-3-642-68123-3_2. ISBN 978-3-642-68125-7. PMID 6269805.
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