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

HJ Lamble, CC Milburn, Garry Lindsay Taylor, DW Hough, MJ Danson

Research output: Other contribution

63 Citations (Scopus)

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
Volume576
DOIs
Publication statusPublished - 8 Oct 2004

Keywords

  • gluconate dehydratase
  • archaea
  • Entner-Doudoroff pathway
  • metabolic pathway promiscuity
  • Sulfolobus solfataricus
  • ARCHAEBACTERIUM SULFOLOBUS
  • ENZYMATIC-ACTIVITIES
  • ENOLASE SUPERFAMILY
  • GLYCOLYTIC PATHWAYS
  • ASPERGILLUS-NIGER
  • GLUCOSE
  • METABOLISM
  • EVOLUTION
  • GLYCOSIDASE
  • DEGRADATION

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