Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus

F J Lamble, C C Milburn, G L Taylor, D W Hough, M J Danson

Research output: Contribution to journalArticle

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Abstract

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 95degreesC 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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)133-136
Number of pages4
JournalFEBS Letters
Volume576
Issue number1-2
DOIs
Publication statusPublished - 2004

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gluconate dehydratase
Sulfolobus solfataricus
galactonate dehydratase
Glucose 1-Dehydrogenase
Archaea
Cell Extracts
Galactose
Metabolism
Half-Life
Monomers
Glucose
Substrates
Enzymes

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Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus. / Lamble, F J; Milburn, C C; Taylor, G L; Hough, D W; Danson, M J.

In: FEBS Letters, Vol. 576, No. 1-2, 2004, p. 133-136.

Research output: Contribution to journalArticle

Lamble, F J ; Milburn, C C ; Taylor, G L ; Hough, D W ; Danson, M J. / Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus. In: FEBS Letters. 2004 ; Vol. 576, No. 1-2. pp. 133-136.
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