the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
the catalytic activity of the protein is investigated by performing indirect enzyme assays using arabinonate dehydratase with D-arabinonate as a substrate. A 50% decrease in the yield of 2-dehydro-3-deoxy-D-arabinonate is observed when both enzymes are co-incubated in the presence of Mg2+. Given the fact that D-arabinonate is converted to 2-oxoglutarate in D-arabinose cell-free extract, this enzyme is anticipated to be responsible for the dehydration of 2-dehydro-3-deoxy-D-arabinonate to the aldehyde 2,5-dioxopentanoate. Due to the unavailability of 2-dehydro-3-deoxy-D-arabinonate, it is not possible to show this in a direct enzyme assay. 2-Oxoglutarate is produced in an indirect assay using arabinonate dehydratase, the putative 2-dehydro-3-deoxy-D-arabinonate dehydratase and the predicted aldehyde dehydrogenase
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
the catalytic activity of the protein is investigated by performing indirect enzyme assays using arabinonate dehydratase with D-arabinonate as a substrate. A 50% decrease in the yield of 2-dehydro-3-deoxy-D-arabinonate is observed when both enzymes are co-incubated in the presence of Mg2+. Given the fact that D-arabinonate is converted to 2-oxoglutarate in D-arabinose cell-free extract, this enzyme is anticipated to be responsible for the dehydration of 2-dehydro-3-deoxy-D-arabinonate to the aldehyde 2,5-dioxopentanoate. Due to the unavailability of 2-dehydro-3-deoxy-D-arabinonate, it is not possible to show this in a direct enzyme assay. 2-Oxoglutarate is produced in an indirect assay using arabinonate dehydratase, the putative 2-dehydro-3-deoxy-D-arabinonate dehydratase and the predicted aldehyde dehydrogenase
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
crystal structures of complexes of the enzyme with magnesium or calcium ions and either a substrate analog 2-oxobutyrate, or the aldehyde enzyme product 2,5-dioxopentanoate reveal the divalent metal ion in the active site is coordinated octahedrally by three conserved carboxylate residues, a water molecule, and both the carboxylate and the oxo groups of the substrate molecule
multiple sequence alignment analysis of the enzyme indicates the presence of a metal binding site consisting of Glu143, Glu145, and Asp164, which may implicate a metal dependent activity
the 2-ketoglutarate semialdehyde dehydrogenase (KGSADH, Saci_1938) seems not to be essential for growth on pentoses. The deletion mutant of the 2-keto-3-deoxyarabinoate/xylonate dehydratase (KDXD/KDAD) is no longer able to catabolize D-xylose or L-arabinose, suggesting the absence of the aldolase-dependent branch in Sulfolobus acidocaldarius
the 2-ketoglutarate semialdehyde dehydrogenase (KGSADH, Saci_1938) seems not to be essential for growth on pentoses. The deletion mutant of the 2-keto-3-deoxyarabinoate/xylonate dehydratase (KDXD/KDAD) is no longer able to catabolize D-xylose or L-arabinose, suggesting the absence of the aldolase-dependent branch in Sulfolobus acidocaldarius
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of complexes of the enzyme with magnesium or calcium ions and either a substrate analog 2-oxobutyrate, or the aldehyde enzyme product 2,5-dioxopentanoate, 2.1 A resolution
the deletion mutant DELTAKDXD/KDAD of the 2-keto-3-deoxyarabinoate/xylonate dehydratase is no longer able to catabolize D-xylose or L-arabinose, suggesting the absence of the aldolase-dependent branch in Sulfolobus acidocaldarius. In the DELTAKDXD/KDAD mutant, no KDXD/KDAD activity is detected on the four different carbon and energy sources, confirming the absence of an alternative pathway/enzyme for KDX/KDA conversion under these conditions in Sulfolobus acidocaldarius strain MW001
the deletion mutant DELTAKDXD/KDAD of the 2-keto-3-deoxyarabinoate/xylonate dehydratase is no longer able to catabolize D-xylose or L-arabinose, suggesting the absence of the aldolase-dependent branch in Sulfolobus acidocaldarius. In the DELTAKDXD/KDAD mutant, no KDXD/KDAD activity is detected on the four different carbon and energy sources, confirming the absence of an alternative pathway/enzyme for KDX/KDA conversion under these conditions in Sulfolobus acidocaldarius strain MW001
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the KDXD/KDAD activity in the wild-type MW001 and DELTAKGSADH mutant strains and the DELTAABC-SBP strain is induced to 35 mU/mg when D-xylose or L-arabinose is used as the growth substrate. In the absence of these sugars, i.e., on N-Z-amine alone and on N-Z-amine plus dextrin as the carbon and energy source, only negligible KDXD/KDAD activity is observed
the KDXD/KDAD activity in the wild-type MW001 and DELTAKGSADH mutant strains and the DELTAABC-SBP strain is induced to 35 mU/mg when D-xylose or L-arabinose is used as the growth substrate. In the absence of these sugars, i.e., on N-Z-amine alone and on N-Z-amine plus dextrin as the carbon and energy source, only negligible KDXD/KDAD activity is observed
the KDXD/KDAD activity in the wild-type MW001 and DELTAKGSADH mutant strains and the DELTAABC-SBP strain is induced to 35 mU/mg when D-xylose or L-arabinose is used as the growth substrate. In the absence of these sugars, i.e., on N-Z-amine alone and on N-Z-amine plus dextrin as the carbon and energy source, only negligible KDXD/KDAD activity is observed
Brouns, S.J.; Barends, T.R.; Worm, P.; Akerboom, J.; Turnbull, A.P.; Salmon, L.; van der Oost, J.
Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features of the FAH superfamily
Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment
Wagner, M.; Shen, L.; Albersmeier, A.; van der Kolk, N.; Kim, S.; Cha, J.; Bräsen, C.; Kalinowski, J.; Siebers, B.; Albers, S.
Sulfolobus acidocaldarius transports pentoses via a carbohydrate uptake transporter 2 (CUT2)-type ABC transporter and metabolizes them through the aldolase-independent Weimberg pathway