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Literature summary for 1.2.1.5 extracted from

  • Kolawole, A.N.; Akinladejo, V.T.; Elekofehinti, O.O.; Akinmoladun, A.C.; Kolawole, A.O.
    Experimental and computational modeling of interaction of kolaviron-kolaflavanone with aldehyde dehydrogenase (2018), Bioorg. Chem., 78, 68-79 .
    View publication on PubMed
Search for more literature for 1.2.1.5

Application

Application Comment Organism
analysis ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy Saccharomyces cerevisiae

Inhibitors

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Saccharomyces cerevisiae
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae
NADP+
-
 Saccharomyces cerevisiae

General Information

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