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