This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ho, K. K. Articles by Weiner, H. Search for Related Content PubMed PubMed Citation Articles by Ho, K. K. Articles by Weiner, H.

Isolation and Characterization of an Aldehyde Dehydrogenase Encoded by the aldB Gene of Escherichia coli

Biochemistry Department, Purdue University, West Lafayette, Indiana¹

Received 18 May 2004/ Accepted 30 October 2004

An aldehyde dehydrogenase was detected in crude cell extracts of Escherichia coli DH5. Growth studies indicated that the aldehyde dehydrogenase activity was growth phase dependent and increased in cells grown with ethanol. The N-terminal amino acid sequence of the purified enzyme identified the latter as an aldehyde dehydrogenase encoded by aldB, which was thought to play a role in the removal of aldehydes and alcohols in cells that were under stress. The purified enzyme showed an estimated molecular mass of 220 ± 8 kDa, consisting of four identical subunits, and preferred to use NADP and acetaldehyde. MgCl₂ increased the activity of the NADP-dependent enzyme with various substrates. A comparison of the effect of Mg²⁺ ions on the bacterial enzyme with the effect of Mg²⁺ ions on human liver mitochondrial aldehyde dehydrogenase revealed that the bacterial enzyme shared kinetic properties with the mammalian enzyme. An R197E mutant of the bacterial enzyme appeared to retain very little NADP-dependent activity on acetaldehyde.

This is journal paper 17531 from the Purdue University Agricultural Experiment Station.

This article has been cited by other articles:

• Perez, J. M., Arenas, F. A., Pradenas, G. A., Sandoval, J. M., Vasquez, C. C. (2008). Escherichia coli YqhD Exhibits Aldehyde Reductase Activity and Protects from the Harmful Effect of Lipid Peroxidation-derived Aldehydes. J. Biol. Chem. 283: 7346-7353 [Abstract] [Full Text]  
• Rodriguez-Zavala, J. S. (2008). Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase. Protein Sci. 17: 563-570 [Abstract] [Full Text]  
• Franchini, A. G., Egli, T. (2006). Global gene expression in Escherichia coli K-12 during short-term and long-term adaptation to glucose-limited continuous culture conditions. Microbiology 152: 2111-2127 [Abstract] [Full Text]  
• Rodriguez-Zavala, J. S., Allali-Hassani, A., Weiner, H. (2006). Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases.. Protein Sci. 15: 1387-1396 [Abstract] [Full Text]