G 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. The transferase catalytic center can hydrolyze α‑1,6 glycosidic bonds. The oligo‑(α1→4)‑(α1→4) glucanotransferase catalytic center is in the C‑terminal half. Oligo‑(α1→4)‑(α1→4) glucanotransferase activity creates a substrate for (α‑1→6) glucosidase. Based on the peaks in the HPLC charts, what do you think is the most likely substrate for the oligo‑(α1→4)‑(α1→4) glucanotransferase catalytic center of glycogen debranching enzyme? maltotetraosyl and glucosyl residues 6‑O‑α‑glucosyl cyclomaltoheptaose maltosyl and maltotriosyl residues maltoheptaosyl and maltooctaosyl residues cyclomaltoheptaose (β‑cyclodextrin)

A gene, treX, encoding a debranching enzyme previously cloned from the trehalose biosynthesis gene cluster of Sulfolobus solfataricus P2 was expressed in Escherichia coli as a His-tagged protein and the biochemical properties were studied. The specific activity of the S. solfataricus debranching enzyme (TreX) was highest at 75°C and pH 5.5. The enzyme exhibited hydrolysing activity toward α-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, and glycogen was the preferred substrate. TreX has a high specificity for hydrolysis of maltohexaosyl α-1,6-β-cyclodextrin, indicating the high preference for side chains consisting of 6 glucose residues or more. The enzyme also exhibited 4-α-sulfoxide-glucan transferase activity, catalysing transfer of α-1,4-glucan oligosaccharides from one chain to another. Dimethyl sulfoxide (10%, v/v) increased the hydrolytic activity of TreX. Gel permeation chromatography and sedimentation equilibrium analytical ultracentrifugation revealed that the enzyme exists mostly as a dimer at pH 7.0, and as a mixture of dimers and tetramers at pH 5.5. Interestingly, TreX existed as a tetramer in the presence of DMSO at pH 5.5–6.5. The tetramer showed a 4-fold higher catalytic efficiency than the dimer. The enzyme catalysed not only intermolecular trans-glycosylation of malto-oligosaccharides (disproportionation) to produce linear α-1,4-glucans, but also intramolecular trans-glycosylation of glycogen. The results presented in this study indicated that TreX may be associated with glycogen metabolism by selective cleavage of the outer side chain.

Explanation: As explained above, i connotes the underline attention ascribed to the tasks.

h let me think

2h2o2--> 2h2o + o2

this reaction is of the spontaneous decomposition of hydrogen peroxide down into water and oxygen.

add 2 molecules of hydrogen peroxide and 2 molecules of water. since oxygen is naturally diatomic, the total number of atoms of each element is now the same on both sides of the equation so it is balanced.

this may not be entirely correct but let me know.