Purification and characterization of an iron-containing alcohol dehydrogenase in extremely thermophilic bacterium Thermotoga hypogea.

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  • Author(s): Ying X;Ying X; Wang Y; Badiei HR; Karanassios V; Ma K
  • Source:
    Archives of microbiology [Arch Microbiol] 2007 Jun; Vol. 187 (6), pp. 499-510. Date of Electronic Publication: 2007 Feb 10.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Springer-Verlag Country of Publication: Germany NLM ID: 0410427 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0302-8933 (Print) Linking ISSN: 03028933 NLM ISO Abbreviation: Arch Microbiol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Berlin, New York, Springer-Verlag.
    • Subject Terms:
      Alcohol Dehydrogenase*/chemistry ; Alcohol Dehydrogenase*/genetics ; Alcohol Dehydrogenase*/isolation & purification ; Hot Temperature*; Gram-Negative Anaerobic Bacteria/*enzymology ; Iron/*analysis; Amino Acid Sequence ; Enzyme Stability ; Gene Expression Regulation, Bacterial ; Gram-Negative Anaerobic Bacteria/genetics ; Gram-Negative Anaerobic Bacteria/growth & development ; Hydrogen-Ion Concentration ; Kinetics ; Molecular Sequence Data ; Oxygen/pharmacology ; Substrate Specificity
    • Abstract:
      Thermotoga hypogea is an extremely thermophilic anaerobic bacterium capable of growing at 90 degrees C. It uses carbohydrates and peptides as carbon and energy sources to produce acetate, CO(2), H(2), L-alanine and ethanol as end products. Alcohol dehydrogenase activity was found to be present in the soluble fraction of T. hypogea. The alcohol dehydrogenase was purified to homogeneity, which appeared to be a homodimer with a subunit molecular mass of 40 +/- 1 kDa revealed by SDS-PAGE analyses. A fully active enzyme contained iron of 1.02 +/- 0.06 g-atoms/subunit. It was oxygen sensitive; however, loss of enzyme activity by exposure to oxygen could be recovered by incubation with dithiothreitol and Fe(2+). The enzyme was thermostable with a half-life of about 10 h at 70 degrees C, and its catalytic activity increased along with the rise of temperature up to 95 degrees C. Optimal pH values for production and oxidation of alcohol were 8.0 and 11.0, respectively. The enzyme had a broad specificity to use primary alcohols and aldehydes as substrates. Apparent K (m) values for ethanol and 1-butanol were much higher than that of acetaldehyde and butyraldehyde. It was concluded that the physiological role of this enzyme is likely to catalyze the reduction of aldehydes to alcohols.
    • Accession Number:
      E1UOL152H7 (Iron)
      EC 1.1.1.1 (Alcohol Dehydrogenase)
      S88TT14065 (Oxygen)
    • Publication Date:
      Date Created: 20070213 Date Completed: 20071009 Latest Revision: 20131121
    • Publication Date:
      20240829
    • Accession Number:
      10.1007/s00203-007-0217-x
    • Accession Number:
      17294170