Promiscuity in the part‐phosphorylative Entner–Doudoroff pathway of the archaeon Sulfolobus solfataricus
- 19 December 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (30) , 6865-6869
- https://doi.org/10.1016/j.febslet.2005.11.028
Abstract
The hyperthermophilic archaeon Sulfolobus solfataricus metabolises glucose and galactose by a 'promiscuous' non-phosphorylative variant of the Entner-Doudoroff pathway, in which a series of enzymes have sufficient substrate promiscuity to permit the metabolism of both sugars. Recently, it has been proposed that the part-phosphorylative Entner-Doudoroff pathway occurs in parallel in S. solfataricus as an alternative route for glucose metabolism. In this report we demonstrate, by in vitro kinetic studies of D-2-keto-3-deoxygluconate (KDG) kinase and KDG aldolase, that the part-phosphorylative pathway in S. solfataricus is also promiscuous for the metabolism of both glucose and galactose.Keywords
This publication has 26 references indexed in Scilit:
- Gluconate dehydratase from the promiscuous Entner–Doudoroff pathway in Sulfolobus solfataricusFEBS Letters, 2004
- Structure of Thermus thermophilus 2-Keto-3-deoxygluconate Kinase: Evidence for Recognition of an Open Chain SubstrateJournal of Molecular Biology, 2004
- Reconstruction of the Central Carbohydrate Metabolism of Thermoproteus tenax by Use of Genomic and Biochemical DataJournal of Bacteriology, 2004
- Structure and mechanism of a sub-family of enzymes related to N -acetylneuraminate lyase 1 1Edited by F. E. CohenJournal of Molecular Biology, 1997
- Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinasesProtein Science, 1993
- Degradation of some sugars and sugar acids by the nonphosphorylated D‐gluconate pathway in Aspergillus ustusActa Biotechnologica, 1989
- Citric acid cycle enzymes of the archaebacteria: citrate synthase and succinate thiokinaseFEBS Letters, 1985
- Thermoacidophilic Archaebacteria Contain Bacterial-Type Ferredoxins Acting as Electron Acceptors of 2-Oxoacid: Ferredoxin OxidoreductasesEuropean Journal of Biochemistry, 1982
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970