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Gluconate dehydratase from the promiscuous Entner–Doudoroff pathway in Sulfolobus solfataricus
Author(s) -
Lamble Henry J.,
Milburn Christine C.,
Taylor Garry L.,
Hough David W.,
Danson Michael J.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.074
Subject(s) - sulfolobus solfataricus , dehydratase , biochemistry , sulfolobus , aldolase a , enzyme , chemistry , biology , archaea , gene
An investigation has been carried out into gluconate dehydratase from the hyperthermophilic Archaeon Sulfolobus solfataricus . The enzyme has been purified from cell extracts of the organism and found to be responsible for both gluconate and galactonate dehydratase activities. It was shown to be a 45 kDa monomer with a half‐life of 41 min at 95 °C and it exhibited similar catalytic efficiency with both substrates. Taken alongside the recent work on glucose dehydrogenase and 2‐keto‐3‐deoxygluconate aldolase, this report clearly demonstrates that the entire non‐phosphorylative Entner–Doudoroff pathway of S. solfataricus is promiscuous for the metabolism of both glucose and galactose.