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Literature summary for 1.2.1.8 extracted from

  • Munoz-Clares, R.A.; Gonzalez-Segura, L.; Mujica-Jimenez, C.; Contreras-Diaz, L.
    Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol (2003), Chem. Biol. Interact., 143-144, 129-137.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
methyl methanethiosulfonate in absence of ligands, the kinetics of inactivation is biphasic, suggesting the existence of two enzyme conformers differing in the reactivity of their catalytic thiolate. Preincubation with NADH or betaine aldehyde prior to the chemical modification brings about active site rearrangements that result in an import decrease in the inactivation rate. Binding of NAD+ increases the rate of inactivation after prolonged preincubation Amaranthus hypochondriacus
methyl methanethiosulfonate in absence of ligands, the kinetics of inactivation is biphasic, suggesting the existence of two enzyme conformers differing in the reactivity of their catalytic thiolate. Preincubation with coenzyme or the aldehyde prior to the chemical modification brings about active site rearrangements that result in an import decrease in the inactivation rate Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Amaranthus hypochondriacus
-
-
-
Pseudomonas aeruginosa
-
-
-

Oxidation Stability

Oxidation Stability Organism
conformational change induced by coenzyme or the aldehyde might be important for both proper enzyme function and protection against oxidation Pseudomonas aeruginosa
conformational change induced by coenzyme or the aldehyde might be important for both proper enzyme function and protection against oxidation Amaranthus hypochondriacus

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Amaranthus hypochondriacus
-