Identify which of the following statements about human glycogen debranching enzyme are true based on the HPLC results. The(α−1→6)glucosidase catalytic center is in the C-terminal half. Oligo-(α∣→4)−(α∣→4)glucanotransferase activity creates a substrate for(α−1→6)glucosidase. The oligo-(α1→4)−(α1→4)glucanotransferase catalytic center is in the C-terminal half. The transferase catalytic center can hydrolyzeα−1,6glycosidic bonds. Based on the peaks in the HPL.C charts. what do you think is the most likely substrate for the center of giycogen debranching enzyme? maltotetraosyl and glucosyl residues cyclomaltoheptaose (β-cyclodexirin) 6-O-x-glucosyl fyclomaloheptaose maitoheptaoxyl and maltooctaosyl residues maltosyl and malteriosyl residues

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16-12-2022
Biology

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Identify which of the following statements about human glycogen debranching enzyme are true based on the HPLC results. The(α−1→6)glucosidase catalytic center is in the C-terminal half. Oligo-(α∣→4)−(α∣→4)glucanotransferase activity creates a substrate for(α−1→6)glucosidase. The oligo-(α1→4)−(α1→4)glucanotransferase catalytic center is in the C-terminal half. The transferase catalytic center can hydrolyzeα−1,6glycosidic bonds. Based on the peaks in the HPL.C charts. what do you think is the most likely substrate for the center of giycogen debranching enzyme? maltotetraosyl and glucosyl residues cyclomaltoheptaose (β-cyclodexirin) 6-O-x-glucosyl fyclomaloheptaose maitoheptaoxyl and maltooctaosyl residues maltosyl and malteriosyl residues

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jaspreetsharma jaspreetsharma · Answer 1 · 2022-12-20T03:14:36-05:00

A debranching enzyme, encoded by the gene treX, was synthesized in Escherichia coli as a His-tagged protein, and its biochemical properties were examined. The gene treX was previously cloned from the Sulfolobus solfataricus P2 trehalose biosynthetic gene cluster.

At pH 5.5 and 75°C, the S. solfataricus debranching enzyme (TreX) had its highest level of specific activity. Although pullulan, amylopectin, and other branching substrates with -1,6-glycosidic linkages exhibited hydrolyzing activity toward the enzyme, glycogen remained its preferred substrate. TreX hydrolyzes maltohexaosyl 1,6-cyclodextrin very specifically, showing a clear preference for side chains containing six or more glucose residues. The enzyme also exhibited 4-sulfoxide-glucan transferase activity, which catalyzes the movement of 1,4-glucan oligosaccharides from one chain to another. Dimethyl sulfoxide improved the hydrolytic activity of TreX. Analytical ultracentrifugation and sedimentation equilibrium analytical gel permeation techniques were used to determine that the enzyme exists mostly as a dimer at pH 7.0 and as a mixture of dimers and tetramers at pH 5.5. Interesting to notice is that TreX could form a tetramer at pH 5.5–6.5 when DMSO is present. The tetramer's catalytic efficiency was four times higher than the dimer's. The enzyme also catalyzed the intermolecular trans-glycosylation of malto-oligosaccharides (disproportionation) to produce linear -1,4-glucans in addition to the intramolecular trans-glycosylation of glycogen. The results of this study revealed that TreX might alter glycogen metabolism by cleaving the outer side chain in a specific manner.

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