Article
A proposal for the Mg2+ binding site of P-type ion motive ATPases and the mechanism of phosphoryl group transfer.
Biochemistry - 1 Jul 1997
Kasho V N, Stengelin M, Smirnova I N, Faller L D
Abstract excerpt
Mutations of D586 in the DPPR sequence of sodium pump decrease the enzyme's affinity for inorganic phosphate [Farley R. A., Heart, E., Kabalin, M., Putnam, D., Wang, K., Kasho, V. N., and Faller, L. D. (1997) Biochemistry 36, 941-951]. Therefore, it was proposed that D586 coordinates the Mg2+ req...
Topics
- Adenosine Monophosphate
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Animals
- Binding Sites
- Kinetics
- Magnesium
- Mutation
- Oxygen Radioisotopes
- Phosphates
- Phosphorylation
- Protein Conformation
- Sequence Homology, Amino Acid
- Sodium-Potassium-Exchanging ATPase
- Swine
- Water