|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Transport Energised by P-P Bond Hydrolysis|
|Reactions Classified By Conversion Type → Simple Reactions → Transport Reactions → Transport Energised by P-P Bond Hydrolysis|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
Note that this reaction equation differs from the official Enzyme Commission reaction equations for this EC number.
Reaction Locations: inner membrane (sensu Gram-negative Bacteria)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: K+-transporting ATPase
Enzyme Commission Synonyms: K+-translocating Kdp-ATPase, multi-subunit K+-transport ATPase
Enzyme Commission Summary:
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme of di(heterotetrameric) structure that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
Gassel98: Gassel M, Siebers A, Epstein W, Altendorf K (1998). "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli." Biochim Biophys Acta 1998;1415(1);77-84. PMID: 9858692
Siebers89: Siebers A, Altendorf K (1989). "Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli." J Biol Chem 1989;264(10);5831-8. PMID: 2522440
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