J. Biol. Chem., Vol. 262, Issue 29, 13991-13996, 10, 1987

Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12

L Baldoma and J Aguilar
Department of Biochemistry, School of Pharmacy, University of Barcelona Pedralbes, Spain.

Lactaldehyde dehydrogenase (E.C. 1.2.1.22) of Escherichia coli has been purified to homogeneity. It has four apparently equal subunits (molecular weight 55,000 each) and four NAD binding sites per molecule of native enzyme. The enzyme is inducible, only under aerobic conditions, by at least three different types of molecules, the sugars fucose and rhamnose, the diol ethylene glycol and the amino acid glutamate. The enzyme catalyzes the irreversible oxidation of several aldehydes with a Km in the micromolar range for alpha-hydroxyaldehydes (lactaldehyde, glyceraldehyde, or glycolaldehyde) and a higher Km, in the millimolar range, for the alpha-ketoaldehyde methylglyoxal. It displays substrate inhibition with all these substrates. NAD is the preferential cofactor. The functional and structural features of the enzyme indicate that it is not an isozyme of other E. coli aldehyde dehydrogenases such as glyceraldehyde phosphate dehydrogenase, glycolaldehyde dehydrogenase, or acetaldehyde dehydrogenase. The enzyme, previously described as specific for lactaldehyde, is thus identified as a dehydrogenase with a fairly general role in aldehyde oxidation, and it is probably involved in several metabolic pathways.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. S. Rodriguez-Zavala Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase Protein Sci., March 1, 2008; 17(3): 563 - 570. [Abstract] [Full Text] [PDF]

				K. R. Hristova, R. Schmidt, A. Y. Chakicherla, T. C. Legler, J. Wu, P. S. Chain, K. M. Scow, and S. R. Kane Comparative Transcriptome Analysis of Methylibium petroleiphilum PM1 Exposed to the Fuel Oxygenates Methyl tert-Butyl Ether and Ethanol Appl. Envir. Microbiol., November 15, 2007; 73(22): 7347 - 7357. [Abstract] [Full Text] [PDF]

				L. L. Grochowski, H. Xu, and R. H. White Identification of Lactaldehyde Dehydrogenase in Methanocaldococcus jannaschii and Its Involvement in Production of Lactate for F420 Biosynthesis. J. Bacteriol., April 1, 2006; 188(8): 2836 - 2844. [Abstract] [Full Text] [PDF]

				C. Montella, L. Bellsolell, R. Perez-Luque, J. Badia, L. Baldoma, M. Coll, and J. Aguilar Crystal Structure of an Iron-Dependent Group III Dehydrogenase That Interconverts L-Lactaldehyde and L-1,2-Propanediol in Escherichia coli J. Bacteriol., July 15, 2005; 187(14): 4957 - 4966. [Abstract] [Full Text] [PDF]

				K. K. Ho and H. Weiner Isolation and Characterization of an Aldehyde Dehydrogenase Encoded by the aldB Gene of Escherichia coli J. Bacteriol., February 1, 2005; 187(3): 1067 - 1073. [Abstract] [Full Text] [PDF]

				T. Maeda, I. Yoshinaga, T. Shiba, M. Murakami, A. Wada, and Y. Ishida Cloning and Sequencing of the Gene Encoding an Aldehyde Dehydrogenase That Is Induced by Growing Alteromonas sp. Strain KE10 in a Low Concentration of Organic Nutrients Appl. Envir. Microbiol., May 1, 2000; 66(5): 1883 - 1889. [Abstract] [Full Text]

				M. T. Pellicer, C. Fernandez, J. Badia, J. Aguilar, E. C. C. Lin, and L. Baldoma Cross-induction of glc and ace Operons of Escherichia coli Attributable to Pathway Intersection. CHARACTERIZATION OF THE glc PROMOTER J. Biol. Chem., January 15, 1999; 274(3): 1745 - 1752. [Abstract] [Full Text] [PDF]

				Z. Lu, E. Cabiscol, N. Obradors, J. Tamarit, J. Ros, J. Aguilar, and E. C. C. Lin Evolution of an Escherichia coli Protein with Increased Resistance to Oxidative Stress J. Biol. Chem., April 3, 1998; 273(14): 8308 - 8316. [Abstract] [Full Text] [PDF]