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Archives of Microbiology

, Volume 168, Issue 1, pp 59–67 | Cite as

Properties and primary structure of a thermostable l-malate dehydrogenase from Archaeoglobus fulgidus

  • Anne Siri Langelandsvik
  • I. H. Steen
  • Nils-Kåre Birkeland
  • Torleiv Lien
Original paper

Abstract

A thermostable l-malate dehydrogenase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus was isolated and characterized, and its gene was cloned and sequenced. The enzyme is a homodimer with a molecular mass of 70 kDa and catalyzes preferentially the reduction of oxaloacetic acid with NADH. A. fulgidus l-malate dehydrogenase was stable for 5 h at 90° C, and the half-life at 101° C was 80 min. Thus, A. fulgidus l-malate dehydrogenase is the most thermostable l-malate dehydrogenase characterized to date. Addition of K2HPO4 (1 M) increased the thermal stability by 40%. The primary structure shows a high similarity to l-lactate dehydrogenase from Thermotoga maritima and gram-positive bacteria, and to l-malate dehydrogenase from the archaeon Haloarcula marismortui and other l-lactate-dehydrogenase-like l-malate dehydrogenases.

Key wordsArchaea Archaeoglobus fulgidus Thermophiles Malate dehydrogenase Lactate dehydrogenase Thermostable protein mdh Glycine motif Lactate-dehydrogenase-like malate dehydrogenase 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1997

Authors and Affiliations

  • Anne Siri Langelandsvik
    • 1
  • I. H. Steen
    • 1
  • Nils-Kåre Birkeland
    • 1
  • Torleiv Lien
    • 1
  1. 1.Department of Microbiology, University of Bergen, Jahnebakken 5, N-5020 Bergen, Norway Tel. +47-55-582657; Fax +47-55-589671 e-mail: nils.birkeland@im.uib.noNO

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