scholarly journals Synthesis of Hyperbranched Glycoconjugates by the Combined Action of Potato Phosphorylase and Glycogen Branching Enzyme from Deinococcus geothermalis

Polymers ◽  
2012 ◽  
Vol 4 (1) ◽  
pp. 674-690 ◽  
Author(s):  
Jeroen van der Vlist ◽  
Martin Faber ◽  
Lizette Loen ◽  
Teunis J. Dijkman ◽  
Lia A. T. W. Asri ◽  
...  
Keyword(s):  
Branching Enzyme ◽  
Deinococcus Geothermalis ◽  
Combined Action ◽  
Glycogen Branching Enzyme

Neonatal type IV glycogen storage disease associated with “null” mutations in glycogen branching enzyme 1

2004 ◽  
Vol 145 (5) ◽  
pp. 705-709 ◽  
Author(s):  
Andreas R. Janecke ◽  
Susanne Dertinger ◽  
Uwe-Peter Ketelsen ◽  
Lothar Bereuter ◽  
Burkhard Simma ◽  
...  
Keyword(s):  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Glycogen Storage ◽  
Branching Enzyme ◽  
Type Iv ◽  
Glycogen Branching Enzyme

scholarly journals GLC3 and GHA1 of Saccharomyces cerevisiae are allelic and encode the glycogen branching enzyme.

1992 ◽  
Vol 12 (1) ◽  
pp. 22-29 ◽  
Author(s):  
D W Rowen ◽  
M Meinke ◽  
D C LaPorte
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Glycogen Metabolism ◽  
Striking Difference ◽  
Branching Enzyme ◽  
Yeast Saccharomyces Cerevisiae ◽  
Storage Carbohydrate ◽  
Functional Product ◽  
Cloned Gene ◽  
Transposon Insertions ◽  
Glycogen Branching Enzyme

In the yeast Saccharomyces cerevisiae, glycogen serves as a major storage carbohydrate. In a previous study, mutants with altered glycogen metabolism were isolated on the basis of the altered iodine-staining properties of colonies. We found that when glycogen produced by strains carrying the glc-1p (previously called gha1-1) mutation is stained with iodine, the absorption spectrum resembles that of starch rather than that of glycogen, suggesting that this mutation might reduce the level of branching in the glycogen particles. Indeed, glycogen branching activity was undetectable in extracts from a glc3-1p strain but was elevated in strains which expressed GLC3 from a high-copy-number plasmid. These observations suggest that GLC3 encodes the glycogen branching enzyme. In contrast to glc3-1p, the glc3-4 mutation greatly reduces the ability of yeast to accumulate glycogen. These mutations appear to be allelic despite the striking difference in the phenotypes which they produce. The GLC3 clone complemented both glc3-1p and glc3-4. Deletions and transposon insertions in this clone had parallel effects on its ability to complement glc3-1p and glc3-4. Finally, a fragment of the cloned gene was able to direct the repair of both glc3-1p and glc3-4. Disruption of GLC3 yielded the glycogen-deficient phenotype, indicating that glycogen deficiency is the null phenotype. The glc3-1p allele appears to encode a partially functional product, since it is dominant over glc3-4 but recessive to GLC3. These observations suggest that the ability to introduce branches into glycogen greatly increases the ability of the cell to accumulate that polysaccharide. Northern (RNA) blot analysis identified a single mRNA of 2,300 nucleotides that increased in abundance ca. 20-fold as the culture approached stationary phase. It thus appears that the expression of GLC3 is regulated, probably at the level of transcription.

Glycogen branching enzyme deficiency in adult polyglucosan body disease

1993 ◽  
Vol 33 (1) ◽  
pp. 88-93 ◽  
Author(s):  
Claudio Bruno ◽  
Serenella Servidei ◽  
Sara Shanske ◽  
George Karpati ◽  
Stirling Carpenter ◽  
...  
Keyword(s):  
Enzyme Deficiency ◽  
Branching Enzyme ◽  
Polyglucosan Body ◽  
Adult Polyglucosan Body Disease ◽  
Glycogen Branching Enzyme

Human Skeletal Muscle Glycogen Branching Enzyme Activities with Exercise and Training

1974 ◽  
Vol 52 (1) ◽  
pp. 119-122 ◽  
Author(s):  
A. W. Taylor ◽  
J. Stothart ◽  
M. A. Booth ◽  
R. Thayer ◽  
S. Rao
Keyword(s):  
Skeletal Muscle ◽  
Muscle Glycogen ◽  
Enzyme Activities ◽  
Vastus Lateralis ◽  
Submaximal Exercise ◽  
Relative Fitness ◽  
Vastus Lateralis Muscle ◽  
Branching Enzyme ◽  
Skeletal Muscle Glycogen ◽  
Glycogen Branching Enzyme

Sixteen healthy male subjects classified as sedentary (8) or active (8), exercised to exhaustion on a bicycle ergometer at a load requiring 70% of their maximal aerobic capacity. Biopsy samples of the vastus lateralis muscle were taken at rest and at the time of fatigue. A 12 week training program increased skeletal muscle glycogen content and branching enzyme activities twofold. The exhaustive submaximal exercise reduced the glycogen levels of the trained group to values similar to the fatigue levels of the non-trained subjects. Skeletal muscle glycogen branching enzyme activities decreased with submaximal exercise to fatigue in all groups. Maximal exercise to fatigue resulted in small increases in the activities of the enzyme. The results of the present study and a previous study (Taylor et al. 1972. Can. J. Physiol. Pharmacol. 50, 411–415) indicate that the activities of the glycogen synthesizing enzymes are highly correlated with the skeletal muscle resting glycogen concentration and the relative fitness of the subjects.

scholarly journals Polyglucosan neurotoxicity caused by glycogen branching enzyme deficiency can be reversed by inhibition of glycogen synthase

2013 ◽  
Vol 127 (1) ◽  
pp. 101-113 ◽  
Author(s):  
Or Kakhlon ◽  
Hava Glickstein ◽  
Naomi Feinstein ◽  
Yan Liu ◽  
Otto Baba ◽  
...  
Keyword(s):  
Glycogen Synthase ◽  
Enzyme Deficiency ◽  
Branching Enzyme ◽  
Glycogen Branching Enzyme

The glgB-encoded glycogen branching enzyme is essential for glycogen accumulation in Corynebacterium glutamicum

Microbiology ◽  
2011 ◽  
Vol 157 (11) ◽  
pp. 3243-3251 ◽  
Author(s):  
Gerd M. Seibold ◽  
Katrin J. Breitinger ◽  
Raoul Kempkes ◽  
Leonard Both ◽  
Matthias Krämer ◽  
...  
Keyword(s):  
Corynebacterium Glutamicum ◽  
Gene Product ◽  
Glycogen Synthase ◽  
Exponential Growth Phase ◽  
Branching Enzyme ◽  
Glycogen Accumulation ◽  
Glycosidic Bonds ◽  
Its Gene ◽  
Glycogen Branching Enzyme

Corynebacterium glutamicum transiently accumulates glycogen as carbon capacitor during the early exponential growth phase in media containing carbohydrates. In some bacteria glycogen is synthesized by the consecutive action of ADP-glucose pyrophosphorylase (GlgC), glycogen synthase (GlgA) and glycogen branching enzyme (GlgB). GlgC and GlgA of C. glutamicum have been shown to be necessary for glycogen accumulation in this organism. However, although cg1381 has been annotated as the putative C. glutamicum glgB gene, cg1381 and its gene product have not been characterized and their role in transient glycogen accumulation has not yet been investigated. We show here that the cg1381 gene product of C. glutamicum catalyses the formation of α-1,6-glycosidic bonds in polysaccharides and thus represents a glycogen branching enzyme. RT-PCR experiments revealed glgB to be co-transcribed with glgE, probably encoding a maltosyltransferase. Promoter activity assays with the glgE promoter region revealed carbon-source-dependent expression of the glgEB operon. Characterization of the growth and glycogen content of glgB-deficient and glgB-overexpressing strains showed that the glycogen branching enzyme GlgB is essential for glycogen formation in C. glutamicum. Taken together these results suggest that an interplay of the enzymes GlgC, GlgA and GlgB is not essential for growth, but is required for synthesis of the transient carbon capacitor glycogen in C. glutamicum.

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