Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Alec+Lester Proteopedia - User contributions [en] 2026-09-14T11:58:42Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225299 Sandbox Reserved 301 2011-04-04T17:41:10Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]] <br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Conserved_residues/1'>Conserved Residues</scene> <ref name="Abad"/>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutagensis an chemical motification revealed that Tyr300 and Glu459 to be conserved specifically to E.''coli''.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225298 Sandbox Reserved 301 2011-04-04T17:38:46Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]] <br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutagensis an chemical motification revealed that Tyr300 and Glu459 to be conserved specifically to E.''coli''.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225296 Sandbox Reserved 301 2011-04-04T17:37:35Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]] <br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>.<br /> These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutagensis an chemical motification revealed that Tyr300 and Glu459 to be conserved specifically to E.''coli'' BE <ref name="Abad"/>.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225292 Sandbox Reserved 301 2011-04-04T17:35:45Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]] <br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>.<br /> These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. coli Branching Enzyme in order for the enzymatic activity to be functional<ref name="Abad"/>.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225291 Sandbox Reserved 301 2011-04-04T17:34:10Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]] <br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>.<br /> These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. coli Branching Enzyme in order for the enzymatic activity to be functional <ref name="Abad"/>.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225289 Sandbox Reserved 301 2011-04-04T17:31:04Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]] <br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>.<br /> The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>.<br /> These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>.<br /> Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional<ref name="Abad"/>.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225288 Sandbox Reserved 301 2011-04-04T17:29:12Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png |thumb|left||Glycogen structure by [http://commons.wikimedia.org/wiki/User:Mikael_H%C3%A4ggstr%C3%B6m Mikael Haggstrom]]]<br /> <br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV)<ref name="Abad"/>. This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer<ref name="Abad"/>. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system<ref name="Abad"/>.<br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes<ref name="Abad"/>. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre<ref name="Abad"/>.<br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes<ref name="Abad"/>.<br /> The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain <ref name="Abad"/>.<br /> <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred<ref name="Abad"/>. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units<ref name="Abad"/>.<br /> <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity<ref name="Abad"/>.<br /> <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene> <ref name="Abad"/>.<br /> These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms<ref name="Abad"/>.<br /> Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional<ref name="Abad"/>.<br /> <br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225285 Sandbox Reserved 301 2011-04-04T17:25:05Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> [[Image:300px-Glycogen_structure_svg.png | Glycogen structure]]<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=File:300px-Glycogen_structure_svg.png&diff=1225284 File:300px-Glycogen structure svg.png 2011-04-04T17:23:24Z

<p>Alec Lester: </p> <hr /> <div>== Licensing ==<br /> {{cc-by-sa-3.0}}</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225282 Sandbox Reserved 301 2011-04-04T17:21:44Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen<ref name="Abad">PMID:12196524</ref>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225280 Sandbox Reserved 301 2011-04-04T17:20:59Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen <ref name="Abad"/>. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="Abad"/>. The branching enzyme belongs to the a-amylase family of enzymes<ref name="Abad"/>.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides<ref name="Abad"/>. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position<ref name="Abad"/>. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1)<ref name="Abad"/>.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225278 Sandbox Reserved 301 2011-04-04T17:19:33Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen <ref name="1m7x">. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site <ref name="1m7x">. The branching enzyme belongs to the a-amylase family of enzymes<ref name="1m7x">.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell (as shown in Figure 1).<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> =References=<br /> <references/><br /> <ref name="1m7x">[http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225276 Sandbox Reserved 301 2011-04-04T17:13:20Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> <scene name='Sandbox_Reserved_301/Conserved_residues/1'>Conserved Residues</scene><br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225272 Sandbox Reserved 301 2011-04-04T17:08:35Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> <scene name='Sandbox_Reserved_301/Conserved_residues/1'>Conserved Residues</scene>=References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225222 Sandbox Reserved 301 2011-04-04T15:38:20Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='E.''coli'' localized residues' /><br /> <br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225216 Sandbox Reserved 301 2011-04-04T15:32:05Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Residues</scene>. These conserved residues are conserved among members of the a-amylase fmaily including Branching enzymes from various organisms. Studies involving site-directed mutanegensis and chemical modifications revealed that Try300 and Glu459 have to be conserved specifically to E. ''coli'' Branching enzyme in order for the enzymatic activity to be functional.<br /> <br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225213 Sandbox Reserved 301 2011-04-04T15:27:02Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> The NH2-terminal domain is involved in determining the size of the chain transferred. This domain helps determine the unique feature of the action of the branching enzyme lies to the specificity for the length of the glucan chain transferred. E. coli Branching Enzyme prefers to transfer shorter chains between 5 and 16 glucose units. <br /> ==Carboxyl-Terminal Domain==<br /> The COOH-terminal domain is involved in substrate preference and catalytic capacity. <br /> <br /> ==Central (a/b) Barrel Catalytic Domain==<br /> Based on analysis of biochemical and X-Ray structures of apo- (without a substrate bound) and substrate-bound a-amylase and CGT, the catalytic center of of these enzymes have been localized to the residues Tyr300, Asp335, His340, Arg403, Asp405, Glu458, and Asp526 in the E. ''coli'' as shown in <scene name='Sandbox_Reserved_301/Gbe1/2'>Conserved Area</scene>. <br /> <br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225205 Sandbox Reserved 301 2011-04-04T14:42:49Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres of a-amylase, isoamylase, CGT with the branching enzyme show that these enzymes have a common (a/b) barrel domain that contains the enzyme's catalytic centre. <br /> <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene><br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =Domains=<br /> Braching enzyme is divided in three domains based on the prediction of secondary structure and smiliarities of amylotic family of enzymes. The three domains consist of an amino-terminal domain, a carboxyl-terminal domain, and a central (a/b) barrel catalytic domain. <br /> ==Amino-Terminal Domain==<br /> ==Carboxyl-Terminal Domain==<br /> ==Central (a/b) Barrel Catalytic Domain==<br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225202 Sandbox Reserved 301 2011-04-04T14:33:26Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> E. coli Branching enzyme belongs to the a-amylase family of enzymes. Members of this group include a-amylase, pullulanase/isoamylase, cyclodextrin glucanotransferase (CGT), and branching enzymes. Analyzing X-ray structres, a-amylase, isoamylase, and <br /> <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene><br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =Domains=<br /> <br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225201 Sandbox Reserved 301 2011-04-04T14:25:22Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen. The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene><br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =Function=<br /> Branching Enzymes contributes to the structure of startch in plants and glycogen in animals and bacteria by catalyzing the formation of a-1,6 brach points in the polysaccharides. The polysaccharide is cleaved at the a-1,4 glucosidic linkage, yidleing a non-reducing end oligosaccharide chain and subsequent attachment to the a-1,6 position. Branching of polysaccharides increased the number of non-reducing ends which makes glycogen more reactive to synthesis and digestion, alos essential for assuring its solubility in the cell.<br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =Family=<br /> =Domains=<br /> <br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1225193 Sandbox Reserved 301 2011-04-04T13:36:57Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> Escherichia coli Branching Enzyme (BE) (1,4-a-glucan 6-glucosyltransferase)catalyzes the formation of a-1,6 branch points of glycogen (similar process for start with starch branching points). The enzyme contains three domains: a NH2-terminal seven stranded b-sandwich domain, a COOH-terminal domain, and a central a/b-barrel domain containing the enzyme active site. The branching enzyme belongs to the a-amylase family of enzymes.<br /> __TOC__<br /> <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene><br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =Glyogen Storage Disease type IV=<br /> <br /> Mutations in the gene of Branching Enzyme can result in the accumulation of insoluble glycogen in the cell known as Glycogen Storage Disease type IV (GSD-IV). This results in an impaired enzyme which prevents the formation of branch points in glycogen, producing an insoluble polymer. Different forms of GSD-Iv affects the liver, muscular tissue, and/or the central and peripheral nervous system. <br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1200909 Sandbox Reserved 301 2011-03-04T04:42:54Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> __TOC__<br /> <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene><br /> <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1200897 Sandbox Reserved 301 2011-03-04T04:02:42Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> {{STRUCTURE_1m7x|PDB=1m7x|SCENE=}}<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> __TOC__<br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester https://proteopedia.org/index.php?title=Sandbox_Reserved_301&diff=1200892 Sandbox Reserved 301 2011-03-04T03:54:42Z

<p>Alec Lester: </p> <hr /> <div><br /> {{Template:Sandbox_Reserved_BCMB307}}<br /> <br /> =Introduction=<br /> <ref name="Abad">PMID:12196524</ref><br /> <ref name="Abad"/><br /> __TOC__<br /> =References=<br /> <references/><br /> [http://www.wikipedia.org E.ColiBranchingEnzyme]</div>

Alec Lester