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High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis.
The hyperthermophilic marine archaeon Thermococcus litoralis exhibits high-affinity transport activity for maltose and trehalose at 85 degrees C. The K(m) for maltose transport was 22 nM, and thatExpand
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Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes.
Maltose metabolism was investigated in the hyperthermophilic archaeon Thermococcus litoralis. Maltose was degraded by the concerted action of 4-alpha-glucanotransferase and maltodextrin phosphorylaseExpand
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MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase).
The Escherichia coli maltose system consists of a number of genes whose products are involved in the uptake and metabolism of maltose and maltodextrins. MalT is the central positive gene activator ofExpand
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Molecular characterization of glucokinase from Escherichia coli K-12.
glk, the structural gene for glucokinase of Escherichia coli, was cloned and sequenced. Overexpression of glk resulted in the synthesis of a cytoplasmic protein with a molecular weight of 35,000. TheExpand
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Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system.
The maltose system in Escherichia coli consists of cell envelope-associated proteins and enzymes that catalyze the uptake and utilization of maltose and alpha,1-4-linked maltodextrins. The presenceExpand
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Thermostabilization of Proteins by Diglycerol Phosphate, a New Compatible Solute from the HyperthermophileArchaeoglobus fulgidus
ABSTRACT Diglycerol phosphate accumulates under salt stress in the archaeonArchaeoglobus fulgidus (L. O. Martins, R. Huber, H. Huber, K. O. Stetter, M. S. da Costa, and H. Santos, Appl. Environ.Expand
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Network regulation of the Escherichia coli maltose system.
The genes of the Escherichia coli maltose regulon are controlled by MalT, the specific transcriptional activator which, together with the inducer maltotriose and ATP, is essential for mal geneExpand
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X‐ray structure of MalY from Escherichia coli: a pyridoxal 5′‐phosphate‐dependent enzyme acting as a modulator in mal gene expression
MalY represents a bifunctional pyridoxal 5′‐phosphate‐dependent enzyme acting as a β‐cystathionase and as a repressor of the maltose regulon. Here we present the crystal structures of wild‐type andExpand
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Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity.
malQ mutants of Escherichia coli lacking amylomaltase cannot grow on maltose. They express the maltose system constitutively and are sensitive to maltose when grown on another carbon source. In anExpand
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The MalT-dependent and malZ-encoded Maltodextrin Glucosidase of Escherichia coli Can Be Converted into a Dextrinyltransferase by a Single Mutation (*)
malZ is a member of the mal regulon. It is controlled by MalT, the transcriptional activator of the maltose system. MalZ has been purified and identified as an enzyme hydrolyzing maltotriose andExpand
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