Sandbox Reserved 338: Difference between revisions

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TreX functions to debranch the side chains of glycogen into maltodextrin, and subsequently TreY and TreZ convert the maltodextrin into trehalose <ref name="Woo" /> <ref name="oligomer"/>. The α-1,4-transferase activity is responsible for catalyzing the transfer of glucose residues from one 1,4-α-D-glucan branch to another, while the α-1,6-glycosidase activity is responsible for cleaving the lone glucose in an α-1,6-glycosidic linkage <ref name="lehninger">Nelson, D. and Cox, M. Lehninger Principles of Biochemistry (5th Ed.), W.H. Freeman and Company, New York (2008).</ref> <ref name="isoamylaseglucanotransferase"> PMID: 17485831 </ref>.

TreX functions to debranch the side chains of glycogen into maltodextrin, and subsequently TreY and TreZ convert the maltodextrin into trehalose <ref name="Woo" /> <ref name="oligomer"/>. The α-1,4-transferase activity of TreX is responsible for catalyzing the transfer of glucose residues from one 1,4-α-D-glucan branch to another, while the α-1,6-glycosidase activity is responsible for cleaving the lone glucose in an α-1,6-glycosidic linkage <ref name="lehninger">Nelson, D. and Cox, M. Lehninger Principles of Biochemistry (5th Ed.), W.H. Freeman and Company, New York (2008).</ref> <ref name="isoamylaseglucanotransferase"> PMID: 17485831 </ref>.

TreX is an oligomer, as it exists in a dimeric state and a tetrameric state, both of which exhibit different enzymatic activities. All subunits are identical, where the monomer contains a total of 612 amino acids <ref name="Woo" />. The polypeptide folds into two secondary structures, a β-sandwhich in the N terminal region, comprised of six β-strands and a (β/α)8 – barrel motif in the central domain, comprised of eight parallel α-strands which encircle eight parallel β-strands. The sequence composition of the TreX monomer exhibits a high degree of homology to the isoamylase debranching enzyme of Pseudomona, however the TreX monomer mainly deviates from this similarity in its substrate binding groove and the absence of a calcium ion ligand <ref name="Woo" />.

Sandbox Reserved 338: Difference between revisions

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 <Structure load='2vnc' size='300' frame='true' align='right' scene='Sandbox_Reserved_338/2vnc/1' />
-TreX functions to debranch the side chains of glycogen into maltodextrin, and subsequently TreY and TreZ convert the maltodextrin into trehalose <ref name="Woo" /> <ref name="oligomer"/>. The α-1,4-transferase activity is responsible for catalyzing the transfer of glucose residues from one 1,4-α-D-glucan branch to another, while the α-1,6-glycosidase activity is responsible for cleaving the lone glucose in an α-1,6-glycosidic linkage <ref name="lehninger">Nelson, D. and Cox, M. Lehninger Principles of Biochemistry (5th Ed.), W.H. Freeman and Company, New York (2008).</ref> <ref name="isoamylaseglucanotransferase"> PMID: 17485831 </ref>.
+TreX functions to debranch the side chains of glycogen into maltodextrin, and subsequently TreY and TreZ convert the maltodextrin into trehalose <ref name="Woo" /> <ref name="oligomer"/>. The α-1,4-transferase activity of TreX is responsible for catalyzing the transfer of glucose residues from one 1,4-α-D-glucan branch to another, while the α-1,6-glycosidase activity is responsible for cleaving the lone glucose in an α-1,6-glycosidic linkage <ref name="lehninger">Nelson, D. and Cox, M. Lehninger Principles of Biochemistry (5th Ed.), W.H. Freeman and Company, New York (2008).</ref> <ref name="isoamylaseglucanotransferase"> PMID: 17485831 </ref>.
 TreX is an oligomer, as it exists in a dimeric state and a tetrameric state, both of which exhibit different enzymatic activities. All subunits are identical, where the monomer contains a total of 612 amino acids <ref name="Woo" />.  The polypeptide folds into two secondary structures, a β-sandwhich in the N terminal region, comprised of six β-strands and a (β/α)8 – barrel motif in the central domain, comprised of eight parallel α-strands which encircle eight parallel β-strands. The sequence composition of the TreX monomer exhibits a high degree of homology to the isoamylase debranching enzyme of Pseudomona, however the TreX monomer mainly deviates from this similarity in its substrate binding groove and the absence of a calcium ion ligand <ref name="Woo" />.