An ATP "Synthase" Derived from a Single Structural Domain of Bacterial Histidine Kinase.
Angew Chem Int Ed Engl
; 63(13): e202318503, 2024 03 22.
Article
in En
| MEDLINE
| ID: mdl-38311597
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacteria
/
Bacterial Proteins
Type of study:
Prognostic_studies
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2024
Document type:
Article