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Extremophiles

, Volume 2, Issue 4, pp 439–446 | Cite as

Gentisate 1,2-dioxygenase from Haloferax sp. D1227

  • W. Fu
  • P. Oriel

Abstract

Gentisate 1,2-dioxygenase from the extreme halophile Haloferax sp. D1227 (Hf. D1227) was purified using a three-step procedure. The enzyme was found to be a homotetramer of 42 000 ± 1000 Da subunits, with a native molecular weight of 174 000 ± 6000 Da. The optimal salt concentration, temperature, and pH for enzyme activity were 2 M KCl or NaCl, 45°C, and pH 7.2, respectively. The gene encoding Hf. D1227 gentisate 1,2-dioxygenase was cloned, sequenced, and expressed in Haloferax volcanii. The deduced amino acid sequence exhibited a 9.2% excess acidic over basic amino acids typical of halophilic enzymes. Four novel histidine clusters and a possible extradiol dioxygenase fingerprint region were identified.

Key words Gentisate 1 2-dioxygenase Extreme halophile Archaea Halophilic enzymes Ring-fission dioxygenases 

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Copyright information

© Springer-Verlag Tokyo 1998

Authors and Affiliations

  • W. Fu
    • 1
  • P. Oriel
    • 1
  1. 1.Department of Microbiology, 40 Giltner Hall, Michigan State University, East Lansing, MI 48824-1101, USA Tel. +1-517-353-4664; Fax +1-517-353-8957 e-mail: 23142mgr@msu.eduUS

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