ArticleThe Biochemical journal2007
Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- Investigation of Substrate Specificity in 5-Keto-4-Deoxy-Glucarate Dehydratase and 2-Keto-3-Deoxy-L-Arabinonate Dehydratase.Chembiochem : a European journal of chemical biology · 2026Article
- Metabolic engineering for microbial production of sugar acids.BMC biotechnology · 2025Review
- Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.Biotechnology for biofuels and bioproducts · 2022Review
- Enzymatic Synthesis of 2-Keto-3-Deoxy-6-Phosphogluconate by the 6-Phosphogluconate-Dehydratase FromFrontiers in bioengineering and biotechnology · 2020Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
- DHAP-dependent aldolases from (hyper)thermophiles: biochemistry and applications.Extremophiles : life under extreme conditions · 2014Review
- Multifunctional enzymes in archaea: promiscuity and moonlight.Extremophiles : life under extreme conditions · 2013Review
- Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes.Computational and structural biotechnology journal · 2012Review
- The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate- specific aldolase.Journal of bacteriology · 2010Article
- Improving low-temperature activity of Sulfolobus acidocaldarius 2-keto-3-deoxygluconate aldolase.Archaea (Vancouver, B.C.) · 2009Article
- Characterization of a thermostable dihydrodipicolinate synthase from Thermoanaerobacter tengcongensis.Extremophiles : life under extreme conditions · 2008Article
- Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities.Microbiology and molecular biology reviews : MMBR · 2008Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aldolases are enzymes with potential applications in biosynthesis, depending on their activity, specificity and stability. In the present study, the genomes of Sulfolobus species were screened for aldolases. Two new KDGA [2-keto-3-deoxygluconate (2-oxo-3-deoxygluconate) aldolases] from Sulfolobus acidocaldarius and Sulfolobus tokodaii were identified, overexpressed in Escherichia coli and characterized. Both enzymes were found to have biochemical properties similar to the previously characterized S. solfataricus KDGA, including the condensation of pyruvate and either D,L-glyceraldehyde or D,L-glyceraldehyde 3-phosphate. The crystal structure of S. acidocaldarius KDGA revealed the presence of a novel phosphate-binding motif that allows the formation of multiple hydrogen-bonding interactions with the acceptor substrate, and enables high activity with glyceraldehyde 3-phosphate. Activity analyses with unnatural substrates revealed that these three KDGAs readily accept aldehydes with two to four carbon atoms, and that even aldoses with five carbon atoms are accepted to some extent. Water-mediated interactions permit binding of substrates in multiple conformations in the spacious hydrophilic binding site, and correlate with the observed broad substrate specificity.
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