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Research article

An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates

Catriona L. BUCHANAN, Helen CONNARIS, Michael J. DANSON, Christopher D. REEVE, David W. HOUGH
Biochemical Journal Nov 01, 1999, 343 (3) 563-570; DOI: 10.1042/bj3430563
Catriona L. BUCHANAN
Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
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Helen CONNARIS
Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
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Michael J. DANSON
Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
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Christopher D. REEVE
Avecia LifeScience Molecules, Belasis Avenue, Billingham, Cleveland TS23 1YN, U.K.
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David W. HOUGH
Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
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  • For correspondence: D.W.Hough@bath.ac.uk
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Abstract

Sulfolobus solfataricus is a hyperthermophilic archaeon growing optimally at 80-85 °C. It metabolizes glucose via a novel non-phosphorylated Entner-Doudoroff pathway, in which the reversible C6 to C3 aldol cleavage is catalysed by 2-keto-3-deoxygluconate aldolase (KDG-aldolase), generating pyruvate and glyceraldehyde. Given the ability of such a hyperstable enzyme to catalyse carbon-carbon-bond synthesis with non-phosphorylated metabolites, we report here the cloning and sequencing of the S. solfataricus gene encoding KDG-aldolase, and its expression in Escherichia coli to give fully active enzyme. The recombinant enzyme was purified in a simple two-step procedure, and shown to possess kinetic properties indistinguishable from the enzyme purified from S. solfataricuscells. The KDG-aldolase is a thermostable tetrameric protein with a half-life at 100 °C of 2.5 h, and is equally active with both D- and L-glyceraldehyde. It exhibits sequence similarity to the N-acetylneuraminate lyase superfamily of Schiff-base-dependent aldolases, dehydratases and decarboxylases, and evidence is presented for a similar catalytic mechanism for the archaeal enzyme by substrate-dependent inactivation by reduction with NaBH4.

  • biotransformation
  • CC bond
  • 2-keto-3-deoxygluconate
  • The Biochemical Society, London © 1999
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November 1999

Volume: 343 Issue: 3

Biochemical Journal: 343 (3)
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An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates
Catriona L. BUCHANAN, Helen CONNARIS, Michael J. DANSON, Christopher D. REEVE, David W. HOUGH
Biochemical Journal Nov 1999, 343 (3) 563-570; DOI: 10.1042/bj3430563
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An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates
Catriona L. BUCHANAN, Helen CONNARIS, Michael J. DANSON, Christopher D. REEVE, David W. HOUGH
Biochemical Journal Nov 1999, 343 (3) 563-570; DOI: 10.1042/bj3430563

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Keywords

biotransformation
CC bond
2-keto-3-deoxygluconate

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