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char = e;code = 101
char = .;code = 46
result sql = The ADP-glucose binding site of the Escherichia coli glycogen synthase.
The ADP-glucose binding site of the Escherichia coli glycogen synthase.
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char = ;code = 32
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char = r;code = 114
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char = t;code = 116
char = a;code = 97
char = l;code = 108
char = l;code = 108
char = i;code = 105
char = z;code = 122
char = e;code = 101
char = d;code = 100
char = ;code = 32
char = r;code = 114
char = e;code = 101
char = t;code = 116
char = a;code = 97
char = i;code = 105
char = n;code = 110
char = i;code = 105
char = n;code = 110
char = g;code = 103
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char = G;code = 71
char = T;code = 84
char = -;code = 45
char = B;code = 66
char = ;code = 32
char = g;code = 103
char = l;code = 108
char = y;code = 121
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char = o;code = 111
char = s;code = 115
char = y;code = 121
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char = n;code = 110
char = s;code = 115
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char = e;code = 101
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char = s;code = 115
char = e;code = 101
char = s;code = 115
char = ;code = 32
char = c;code = 99
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char = n;code = 110
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char = e;code = 101
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char = t;code = 116
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char = k;code = 107
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char = g;code = 103
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char = m;code = 109
char = i;code = 105
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char = ;code = 32
char = a;code = 97
char = m;code = 109
char = o;code = 111
char = n;code = 110
char = g;code = 103
char = ;code = 32
char = t;code = 116
char = h;code = 104
char = i;code = 105
char = s;code = 115
char = ;code = 32
char = g;code = 103
char = r;code = 114
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char = u;code = 117
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char = ;code = 32
char = o;code = 111
char = f;code = 102
char = ;code = 32
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char = n;code = 110
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char = y;code = 121
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char = h;code = 104
char = e;code = 101
char = y;code = 121
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char = u;code = 117
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char = e;code = 101
char = ;code = 32
char = d;code = 100
char = i;code = 105
char = f;code = 102
char = f;code = 102
char = e;code = 101
char = r;code = 114
char = e;code = 101
char = n;code = 110
char = t;code = 116
char = ;code = 32
char = s;code = 115
char = u;code = 117
char = b;code = 98
char = s;code = 115
char = t;code = 116
char = r;code = 114
char = a;code = 97
char = t;code = 116
char = e;code = 101
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result sql = Bacterial glycogen/starch synthases are retaining GT-B glycosyltransferases that transfer glucosyl units from ADP-Glc to the non-reducing end of glycogen or starch. We modeled the Escherichia coli glycogen synthase based on the coordinates of the inactive form of the Agrobacterium tumefaciens glycogen synthase and the active form of the maltodextrin phosphorylase, a retaining GT-B glycosyltransferase belonging to a different family. In this model, we identified a set of conserved residues surrounding the sugar nucleotide substrate, and we replaced them with different amino acids by means of site-directed mutagenesis. Kinetic analysis of the mutants revealed the involvement of these residues in ADP-Glc binding. Replacement of Asp21, Asn246 or Tyr355 for Ala decreased the apparent affinity for ADP-Glc 18-, 45-, and 31-fold, respectively. Comparison with other crystallized retaining GT-B glycosyltransferases confirmed the striking similarities among this group of enzymes even though they use different substrates.

Publication: Arch. Biochem. Biophys. 2006 Sep 15 ;453(2)::188-96.
Publication Date: 2006 Sep 15
Study Author(s): Yep, Alejandra;Ballicora, Miguel A;Preiss, Jack;
Institution: Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Shortcut link to this study:
Bacterial glycogen/starch synthases are retaining GT-B glycosyltransferases that transfer glucosyl units from ADP-Glc to the non-reducing end of glycogen or starch. We modeled the Escherichia coli glycogen synthase based on the coordinates of the inactive form of the Agrobacterium tumefaciens glycogen synthase and the active form of the maltodextrin phosphorylase, a retaining GT-B glycosyltransferase belonging to a different family. In this model, we identified a set of conserved residues surrounding the sugar nucleotide substrate, and we replaced them with different amino acids by means of site-directed mutagenesis. Kinetic analysis of the mutants revealed the involvement of these residues in ADP-Glc binding. Replacement of Asp21, Asn246 or Tyr355 for Ala decreased the apparent affinity for ADP-Glc 18-, 45-, and 31-fold, respectively. Comparison with other crystallized retaining GT-B glycosyltransferases confirmed the striking similarities among this group of enzymes even though they use different substrates.
PMID: 16919233

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