Journal
JOURNAL OF BACTERIOLOGY
Volume 187, Issue 3, Pages 1067-1073Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.187.3.1067-1073.2005
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Funding
- NIAAA NIH HHS [R37 AA005812, AA05812, R01 AA005812] Funding Source: Medline
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An aldehyde dehydrogenase was detected in crude cell extracts of Escherichia coli DH5u. 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.
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