title: Kinetic and structural features of betaine aldehyde dehydrogenases: mechanistic and regulatory implications.
abstract: The betaine aldehyde dehydrogenases (BADH; EC 1.2.1.8) are so-called because they catalyze the irreversible NAD(P)(+)-dependent oxidation of betaine aldehyde to glycine betaine, which may function as (i) a very efficient osmoprotectant accumulated by both prokaryotic and eukaryotic organisms to cope with osmotic stress, (ii) a metabolic intermediate in the catabolism of choline in some bacteria such as the pathogen Pseudomonas aeruginosa, or (iii) a methyl donor for methionine synthesis. BADH enzymes can also use as substrates aminoaldehydes and other quaternary ammonium and tertiary sulfonium compounds, thereby participating in polyamine catabolism and in the synthesis of gamma-aminobutyrate, carnitine, and 3-dimethylsulfoniopropionate. This review deals with what is known about the kinetics and structural properties of these enzymes, stressing those properties that have only been found in them and not in other aldehyde dehydrogenases, and discussing their mechanistic and regulatory implications.
authors.affiliation: Departamento de Bioquímica, Facultad de Química, Universidad Nacional Autónoma de México, México DF 04510, México. clares@servidor.unam.mx
authors.forename: Rosario A
authors.initials: RA
authors.lastname: Muñoz-Clares
authors.forename: Angel G
authors.initials: AG
authors.lastname: Díaz-Sánchez
authors.forename: Lilian
authors.initials: L
authors.lastname: González-Segura
authors.forename: Carmina
authors.initials: C
authors.lastname: Montiel
mesh_terms: D050728:Betaine-Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D008958:Models, Molecular; D009711:Nucleotides / Q000494:pharmacology; D011487:Protein Conformation
chemical_list: D004791:Enzyme Inhibitors; D009711:Nucleotides; D050728:Betaine-Aldehyde Dehydrogenase