Any feedback?
Literature summary for 1.2.1.8 extracted from
- Modulation of the reactivity of the essential cysteine residue of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa (2002), Biochem. J., 361, 577-585.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| methyl methanethiosulphonate | pH-dependence of the second-order rate constant of inactivation suggests that at low pH values the essential Cys exists as thiolate by the formation of an ion pair with a positively charged residue | Pseudomonas aeruginosa |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| betaine aldehyde + NADP+ + H2O | the enzyme has evolved a complex mechanism, involving several conformational rearrangements of the active site, to suit the reactivity of the essential thiol to the availability of dinucleotide and sunstrate | Pseudomonas aeruginosa | betaine + NADPH + H+ | - |
ir | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BADH | - |
Pseudomonas aeruginosa |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Pseudomonas aeruginosa | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
