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Literature summary extracted from

  • Gonzalez-Segura, L.; Velasco-Garcia, R.; Munoz-Clares, R.A.
    Modulation of the reactivity of the essential cysteine residue of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa (2002), Biochem. J., 361, 577-585.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.8 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

EC Number Organism UniProt Comment Textmining
1.2.1.8 Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.8 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

EC Number Synonyms Comment Organism
1.2.1.8 BADH
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.8 NADP+
-
 Pseudomonas aeruginosa