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.
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Received: November 19, 1997 / Accepted: May 12, 1998
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Fu, W., Oriel, P. Gentisate 1,2-dioxygenase from Haloferax sp. D1227. Extremophiles 2, 439–446 (1998). https://doi.org/10.1007/s007920050090
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DOI: https://doi.org/10.1007/s007920050090