Alcohol dehydrogenases from thermophilic and hyperthermophilic archaea and bacteria

Helia Radianingtyas, Phillip C. Wright

Research output: Contribution to journalLiterature review

78 Citations (Scopus)

Abstract

Many studies have been undertaken to characterise alcohol dehydrogenases (ADHs) from thermophiles and hyperthermophiles, mainly to better understand their activities and thermostability. To date, there are 20 thermophilic archaeal and 17 thermophilic bacterial strains known to have ADHs or similar enzymes, including the hypothetical proteins. Some of these thermophiles are found to have multiple ADHs, sometimes of different types. A rigid delineation of amino acid sequences amongst currently elucidated thermophilic ADHs and similar proteins is phylogenetically apparent. All are NAD(P)-dependent, with one exception that utilises the cofactor F420 instead. Within the NAD(P)-dependent group, the thermophilic ADHs are orderly clustered as zinc-dependent ADHs, short-chain ADHs, and iron-containing/activated ADHs. Distance matrix calculations reveal that thermophilic ADHs within one type are homologous, with those derived from a single genus often showing high similarities. Elucidation of the enzyme activity and stability, coupled with structure analysis, provides excellent information to explain the relationship between them, and thermophilic ADHs diversity. © 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)593-616
Number of pages24
JournalFEMS Microbiology Reviews
Volume27
Issue number5
DOIs
Publication statusPublished - Dec 2003

Keywords

  • Directed evolution
  • Enzyme activity
  • Protein structure
  • Rational design
  • Thermostability

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