Application | Comment | Organism |
---|---|---|
analysis | ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
kolaflavanone | the enzyme shows crucial non-canonical and non-catalytic interaction with kolaflavanone, a component of kolaviron, and a major bioflavonoid isolated from Garcinia kola (Bitter kola). The enzyme has one binding site for kolaflavanone with a binding constant (Ka) of 25700 l/mol and effective Forster resonance energy transfer (FRET) of 4.87 nm. The bonding process is enthalpically driven and the reaction not spontaneous. The flavonoid bonding slightly perturbed the secondary and tertiary structures of ALDH that is tryptophangated. The interaction is regulated by both diffusion and ionic strength. Kolaflavanone has a marked effect on the ellipticity of ALDH structure. Molecular docking shows that the binding of kolaflavanone is at the active site of ALDH and the participation of some amino acid residues in the complex formation. Protein-ligand interaction analysis, kinetics, detailed overview. The profiles of atomic fluctuations indicates the rigidity of the ligand-binding site during the simulation. With these, ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy. Temperature dependency of ligand-protein binding, Stern-Volmer dynamic quenching constants, and thermodynamic parameters. Binding is reduced by Na+ | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Saccharomyces cerevisiae | - |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Saccharomyces cerevisiae | |
NADP+ | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme ALDH is responsible for catalytic detoxification from aldehyde-induced cytotoxicity. ALDH has been reported to be involved in pseudo-ligandin properties both for nonaldehydic endobiotics and xenobiotics | Saccharomyces cerevisiae |