Claim · model-written summary
Mutating GAPA1 Asn35 into Gly or Arg81 into Leu strongly diminished the ability of GAPA1 to bind SA.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianae0 - Treatment
- mutating GAPA1 Asn35 into Gly or Arg81 into Leue2
- Gene
- GAPA1e2
- Outcome
- ability of the enzyme to bind SAe2
- Direction
- strongly diminishede2
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the A1 isomer of chloroplastic glyceraldehyde 3-phosphate dehydrogenase (GAPA1) from Arabidopsis thaliana binds SA with a KD of 16.7 nM”
e2“mutating GAPA1 Asn35 into Gly or Arg81 into Leu strongly diminished the ability of the enzyme to bind SA”
Title
Deciphering the Binding of Salicylic Acid to Arabidopsis thaliana Chloroplastic GAPDH-A1
Igor Pokotylo; Denis Hellal; Tahar Bouceba; et al. International Journal of Molecular Sciences 2020. doi:10.3390/ijms21134678
Other claims from this paper (8)
- Observation GAPA1 from Arabidopsis thaliana binds salicylic acid with a KD of 16.7 nM.
- Intervention effect Salicylic acid inhibits GAPDH activity in vitro.
- Intervention effect NADH inhibited in a dose-response manner the binding of SA to GAPA1.
- Mechanism Modelling suggests that SA binds to the same site where the pyrimidine group of the NADP+ cofactor fits.
- Observation The molecular docking analysis identified two putative binding pockets for SA on GAPA1.
- Observation Only one surface cavity around Asn35 would efficiently bind SA in the presence of solvent.
- Observation In silico mutagenesis and simulations pointed to the importance of Asn35 and Arg81 in binding SA to GAPA1.
- Mechanism The same cavity that binds SA is responsible for NADP+ binding to GAPA1.