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Journal of Bacteriology, February 2005, p. 1067-1073, Vol. 187, No. 3
0021-9193/05/$08.00+0     doi:10.1128/JB.187.3.1067-1073.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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

Kwok Ki Ho1 and Henry Weiner1*

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{alpha}. 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.

* Corresponding author. Mailing address: Biochemistry Department, Purdue University, West Lafayette, IN 47904-2063. Phone: (765) 494-1650. Fax: (765) 494-7897. E-mail: hweiner{at}purdue.edu.

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

Journal of Bacteriology, February 2005, p. 1067-1073, Vol. 187, No. 3
0021-9193/05/$08.00+0     doi:10.1128/JB.187.3.1067-1073.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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