Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 493, Issue 1, Pages 71-81Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2009.09.006
Keywords
BADH; Kinetic mechanism; NAD(P)H uncompetitive inhibition; Iso-mechanism; NAD(P)H-induced enzyme inactivation; Monovalent cations; Catalytic residues conformation; NAD(P)(+) binding mode; NAD(P)H catalytic role; Cysteine-nicotinamide adducts
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Funding
- Consejo Nacional de Ciencia y Tecnologia, Mexico (CONACYT) [N9209, 37820, 59654]
- Direccion General de Asuntos del Personal Academico, UNAM (DGAPA) [IN210198, IN221001, IN206505, IN20478]
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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. (C) 2009 Elsevier Inc. All rights reserved.
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