Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus.
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 degrees 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.
Department of Biology and Biochemistry, Centre for Extremophile Research, University of Bath, Bath BA2 7AY, UK.
Henry J
HJ
Lamble
Christine C
CC
Milburn
Garry L
GL
Taylor
David W
DW
Hough
Michael J
MJ
Danson
D000595:Amino Acid Sequence; D002384:Catalysis; D002457:Cell Extracts / Q000737:chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005798:Genes, Bacterial; D006207:Half-Life; D006836:Hydro-Lyases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D013696:Temperature
D002457:Cell Extracts; D006836:Hydro-Lyases; C020576:gluconate dehydratase; C019607:galactonate dehydratase