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

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

doi:10.1016/j.febslet.2004.08.074

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

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 language	English
Volume	576
DOIs	https://doi.org/10.1016/j.febslet.2004.08.074
Publication status	Published - 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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10.1016/j.febslet.2004.08.074

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title = "Gluconate Dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus",

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.",

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",

author = "HJ Lamble and CC Milburn and Taylor, {Garry Lindsay} and DW Hough and MJ Danson",

note = "FEBS Letts",

year = "2004",

month = oct,

day = "8",

doi = "10.1016/j.febslet.2004.08.074",

language = "English",

volume = "576",

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AU - Lamble, HJ

AU - Milburn, CC

AU - Taylor, Garry Lindsay

AU - Hough, DW

AU - Danson, MJ

N1 - FEBS Letts

PY - 2004/10/8

Y1 - 2004/10/8

N2 - 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.

AB - 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.

KW - gluconate dehydratase

KW - archaea

KW - Entner-Doudoroff pathway

KW - metabolic pathway promiscuity

KW - Sulfolobus solfataricus

KW - ARCHAEBACTERIUM SULFOLOBUS

KW - ENZYMATIC-ACTIVITIES

KW - ENOLASE SUPERFAMILY

KW - GLYCOLYTIC PATHWAYS

KW - ASPERGILLUS-NIGER

KW - GLUCOSE

KW - METABOLISM

KW - EVOLUTION

KW - GLYCOSIDASE

KW - DEGRADATION

UR - http://www.scopus.com/inward/record.url?scp=4944251746&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2004.08.074

DO - 10.1016/j.febslet.2004.08.074

M3 - Other contribution

VL - 576

ER -

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

Abstract

Keywords

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