ATP-generating activity of the ADP-forming acetyl-CoA synthetase in free-living microaerophilic fornicates, Aduncisulcus paluster and Kipferlia bialata

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ID: 321524
2026
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Abstract
Fornicata is a group of eukaryotes adapted to anaerobic and microaerophilic environments. These organisms generate ATP anaerobically through substrate-level phosphorylation. ADP-forming acetyl-CoA synthetase (ACS) is one of the key enzymes of this process. While ACS characteristics in the parasite Giardia intestinalis have been studied, those in free-living species remain unknown. Here, we investigated the ATP-generating activities of recombinant ACS (rACS) of free-living fornicates Aduncisulcus paluster and Kipferlia bialata and compared them with Gasterophilus intestinalis. All rACSs exhibited the highest activity toward the substrate acetyl-CoA and the next toward n-propionyl-CoA. For acetyl-CoA, rApACS exhibited higher affinity (lower KM) and lower catalytic turnover (kcat) than the other two that displayed comparable kinetic profiles. For n-propionyl-CoA, rApACS also exhibited lower KM and kcat than the other two, while rGiACS exhibited far higher kcat than the other two, indicating that rGiACS could utilize n-propionyl-CoA effectively. For the substrate ADP, rKbACS exhibited the highest kcat among the three. These results suggest that ACSs from free-living fornicates are active ATP-generating enzymes, and that during the evolution of fornicates, the ATP-generating activity has been conserved, while the subtle changes in kinetic properties have occurred on their ACSs.
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Authors T Koganemaru, Yoshitaka Tamura, Yasutaka Hoshi, Keitaro Kume, Tetsuo Hashimoto, Takeshi Nara
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Journal The Journal of Biochemistry
Year 2026
DOI
10.1093/jb/mvag055
URL
https://doi.org/10.1093/jb/mvag055
Keywords Keywords not found

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