Claim · model-written summary
Modelling suggests that SA binds to the same site where the pyrimidine group of the NADP+ cofactor fits.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianae0 - Outcome
- the very sitee4
- Qualifier
- pyrimidine group of the cofactore4
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
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”
e4“modelling suggests that SA binds to the very site where the pyrimidine group of the cofactor fits”
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 Mutating GAPA1 Asn35 into Gly or Arg81 into Leu strongly diminished the ability of GAPA1 to bind SA.
- Intervention effect NADH inhibited in a dose-response manner the binding of SA to GAPA1.
- 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.