Sandbox Reserved 301
From Proteopedia
| Line 8: | Line 8: | ||
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. | 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. | ||
__TOC__ | __TOC__ | ||
| - | <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene> | ||
| - | <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
=Function= | =Function= | ||
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. | 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. | ||
| Line 16: | Line 14: | ||
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. | 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. | ||
=Family= | =Family= | ||
| + | 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 | ||
| + | <scene name='Sandbox_Reserved_301/Gbe1/2'>TextToBeDisplayed</scene> | ||
| + | <Structure load='1m7x' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
=Domains= | =Domains= | ||
Revision as of 14:33, 4 April 2011
| This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
To get started:
More help: Help:Editing |
Introduction
[1] [1] 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.
Contents |
Function
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.
Glyogen Storage Disease type IV
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.
Family
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
|
Domains
References
- ↑ 1.0 1.1 Abad MC, Binderup K, Rios-Steiner J, Arni RK, Preiss J, Geiger JH. The X-ray crystallographic structure of Escherichia coli branching enzyme. J Biol Chem. 2002 Nov 1;277(44):42164-70. Epub 2002 Aug 23. PMID:12196524 doi:10.1074/jbc.M205746200
