{Reference Type}: Journal Article
{Title}: An ATP "Synthase" Derived from a Single Structural Domain of Bacterial Histidine Kinase.
{Author}: Ji S;Zhou Y;Chen J;Yang M;Li C;Liu M;Liu Y;Jiang L;
{Journal}: Angew Chem Int Ed Engl
{Volume}: 63
{Issue}: 13
{Year}: 2024 03 22
{Factor}: 16.823
{DOI}: 10.1002/anie.202318503
{Abstract}: ATP (adenosine triphosphate) is a vital energy source for living organisms, and its biosynthesis and precise concentration regulation often depend on macromolecular machinery composed of protein complexes or complicated multidomain proteins. We have identified a single-domain protein HK853CA derived from bacterial histidine kinases (HK) that can catalyze ATP synthesis efficiently. Here, we explored the reaction mechanism and multiple factors that influence this catalysis through a combination of experimental techniques and molecular simulations. Moreover, we optimized its enzymatic activity and applied it as an ATP replenishment machinery to other ATP-dependent systems. Our results broaden the understanding of ATP biosynthesis and show that the single CA domain can be applied as a new biomolecular catalyst used for ATP supply.