ArticleThe Journal of biological chemistry2008
ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 72 citations in OpenAlex.
- Structures of rotary ATP synthase fromScience advances · 2025Article
- Comparative genome analysis reveals broad phylogenetic and functional diversity within the order Nitrospirales.The ISME journal · 2025Article
- Analysis of Extracellular ATP Distribution in the Intervertebral Disc.Annals of biomedical engineering · 2024Article
- Bile acid fitness determinants of amBio · 2024Article
- Bile acid fitness determinants of abioRxiv : the preprint server for biology · 2023Article
- Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover.Communications biology · 2023Article
- ClC-7 drives intraphagosomal chloride accumulation to support hydrolase activity and phagosome resolution.The Journal of cell biology · 2023Article
- Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.The Journal of biological chemistry · 2023Article
- Rotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?Frontiers in molecular biosciences · 2023Review
- Structures of multisubunit membrane complexes with the CRYO ARM 200.Microscopy (Oxford, England) · 2022Article
- Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.Nature communications · 2022Article
- Adaptation to Varying Salinity inFrontiers in microbiology · 2022Article
- Mechanical inhibition of isolated VeLife · 2020Article
- Metagenomic recovery of two distinct comammox Nitrospira from the terrestrial subsurface.Environmental microbiology · 2019Article
- Cryo-EM reveals distinct conformations ofeLife · 2019Article
- Cryo-EM studies of the rotary HBiophysics and physicobiology · 2019Review
- Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy.Scientific reports · 2018Article
- MgATP hydrolysis destabilizes the interaction between subunit H and yeast VThe Journal of biological chemistry · 2018Article
- Structure and dynamics of rotary VCellular and molecular life sciences : CMLS · 2018Review
- Cryo EM structure of intact rotary HNature communications · 2018Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vacuolar-type H(+)-ATPase (V-ATPase) catalyzes ATP synthesis and hydrolysis coupled with proton translocation across membranes via a rotary motor mechanism. Here we report biochemical and biophysical catalytic properties of V-ATPase from Thermus thermophilus. ATP hydrolysis of V-ATPase was severely inhibited by entrapment of Mg-ADP in the catalytic site. In contrast, the enzyme was very active for ATP synthesis (approximately 70 s(-1)) with the K(m) values for ADP and phosphate being 4.7 +/- 0.5 and 460 +/- 30 microm, respectively. Single molecule observation showed V-ATPase rotated in a 120 degrees stepwise manner, and analysis of dwelling time allowed the binding rate constant k(on) for ATP to be estimated ( approximately 1.1 x 10(6) m(-1) s(-1)), which was much lower than the k(on) (= V(max)/K(m)) for ADP ( approximately 1.4 x 10(7) m(-1) s(-1)). The slower k(on)(ATP) than k(on)(ADP) and strong Mg-ADP inhibition may contribute to prevent wasteful consumption of ATP under in vivo conditions when the proton motive force collapses.
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