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Domain 3:

Metabolism

Glycogen: Biosynthesis and Regulation

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  • Author: Jack Preiss1
  • Editor: Valley Stewart2
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824; 2: University of California, Davis, Davis, CA
  • Received 23 July 2008 Accepted 14 October 2008 Published 26 September 2009
  • Address correspondence to Jack Preiss preiss@msu.edu.
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  • Abstract:

    The accumulation of glycogen occurs in and serovar Typhimurium as well as in many other bacteria. Glycogen will be formed when there is an excess of carbon under conditions in which growth is limited due to the lack of a growth nutrient, e.g., a nitrogen source. The structural genes of the glycogen biosynthetic enzymes of and Typhimurium have been cloned previously, and that has provided insights in the genetic regulation of glycogen synthesis. An important aspect of the regulation of glycogen synthesis is the allosteric regulation of the ADP-Glc PPase. The current information, views, and concepts regarding the regulation of enzyme activity and the expression of the glycogen biosynthetic enzymes are presented in this review. The recent information on the amino acid residues critical for the activity of both glycogen synthase and branching enzyme (BE) is also presented. The residue involved in catalysis in the ADP-Glc PPase was determined by comparing a predicted structure of the enzyme with the known three-dimensional structures of sugar-nucleotide PPase domains. The molecular cloning of the K-12 structural genes greatly facilitated the subsequent study of the genetic regulation of bacterial glycogen biosynthesis. Results from studies of glycogen excess B mutants SG3 and AC70R1, which exhibit enhanced levels of the enzymes in the glycogen synthesis pathway (i.e., they are derepressed mutants), suggested that glycogen synthesis is under negative genetic regulation.

  • Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4

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Sodium Dodecyl Sulfate
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Protein Synthesis RNAs
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Glycogen: Biosynthesis and Regulation

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ecosalplus.4.7.4.citations
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/content/journal/ecosalplus/10.1128/ecosalplus.4.7.4
2009-09-26
2017-09-21

Abstract:

The accumulation of glycogen occurs in and serovar Typhimurium as well as in many other bacteria. Glycogen will be formed when there is an excess of carbon under conditions in which growth is limited due to the lack of a growth nutrient, e.g., a nitrogen source. The structural genes of the glycogen biosynthetic enzymes of and Typhimurium have been cloned previously, and that has provided insights in the genetic regulation of glycogen synthesis. An important aspect of the regulation of glycogen synthesis is the allosteric regulation of the ADP-Glc PPase. The current information, views, and concepts regarding the regulation of enzyme activity and the expression of the glycogen biosynthetic enzymes are presented in this review. The recent information on the amino acid residues critical for the activity of both glycogen synthase and branching enzyme (BE) is also presented. The residue involved in catalysis in the ADP-Glc PPase was determined by comparing a predicted structure of the enzyme with the known three-dimensional structures of sugar-nucleotide PPase domains. The molecular cloning of the K-12 structural genes greatly facilitated the subsequent study of the genetic regulation of bacterial glycogen biosynthesis. Results from studies of glycogen excess B mutants SG3 and AC70R1, which exhibit enhanced levels of the enzymes in the glycogen synthesis pathway (i.e., they are derepressed mutants), suggested that glycogen synthesis is under negative genetic regulation.

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Figures

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Figure 1

Also shown are the nonreducing ends, which are in violet, with the branched glucosyl residue in the α-1,6 linkage in aqua. represents the rest of the glycogen molecule.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Image of Figure 2
Figure 2

Amino acids are represented by the one-letter amino acid code. Only those amino acids that are different in the typhimurium enzyme are shown. Various amino acids in the sequence are underlined and have been shown to be involved in either substrate or allosteric effector binding or are replaced by other amino acids in allosteric mutant enzymes. K39 is involved in the binding of the activator fructose 1,6-bis-P, A44 is replaced by Thr in the allosteric mutant SG14 enzyme ( 54 ), R67 is replaced by Cys in the allosteric mutant CL1136 enzyme ( 55 ), and Y114 has been shown to be involved in the binding of the substrate ATP ( 39 ) and the inhibitor AMP ( 36 , 37 ). D142 has been identified as being involved in catalysis ( 19 ). K195 has been shown to be involved in the binding of the substrate glucose-1-P ( 20 ), P295 is replaced by Ser in the allosteric mutant SG5 enzyme ( 56 ), and G336 is replaced by Asp in the allosteric mutant 618 enzyme ( 29 , 30 , 57 ). All these amino acids are conserved in the serovar Typhimurium ADP-Glc PPase.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Figure 3

The amino acids interacting with the AMP portion of the sugar nucleotide are in red. Those binding with the glucose-1-P portion are in blue.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Figure 4

Conserved critical residues are shown in bold lettering. The sequences were obtained online from NCBI Sequence Viewer version 2.0. , ; SSIII, starch synthase III.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Figure 5

The deviation is calculated for the results from at least two experiments. The data given by high-performance anion-exchange chromatography were processed in the following way: the sum of the integration of peaks 6 to 40 from malto-oligosaccharide corresponds to 100%, and the integration of each peak was calculated as a percentage of that total. D.P is degree of polymerization; i.e., the malto-oligosaccharide size (e.g., maltose has a D.P. of 2, and maltopentaose has a D.P. of 5). Reproduced from reference 91 with permission.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Image of Figure 6
Figure 6

This map was constructed from the sequences obtained from references 40 , 72 , 81 , 82 , 97 , 98 , and 101 . corresponds to aspartate semialdehyde dehydrogenase, encodes the BE, encodes isoamylase, encodes ADP-glucose PPase, encodes glycogen synthase, encodes glycogen phosphorylase, and encodes glycerophosphate dehydrogenase. All the genes are transcribed from left to right (counterclockwise on the genome), except for the gene.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Figure 7

The site was detected by DNase I protection analysis ( 109 ), and that of was derived on the basis of homology to the sequence ( 111 ). The asterisks indicate the conservation in the sequences of the transcripts with the consensus CRP binding site.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Figure 8

The 5′ termini of transcripts are indicated by asterisks, and the best −10 and −35 regions are underlined.

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Figure 9

The CRP binding region was located by mobility shift analysis ( 109 ). Transcripts from wild-type strains of B and K-12 and isogenic glycogen synthesis mutants were examined by S1 nuclease protection analysis ( 109 ).

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Tables

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Table 1

Allosteric kinetic constants of and serovar Typhimurium LT2 ADP-Glc PPases and glycogen accumulation rates

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Table 2

Results of mutation of amino acids necessary for binding of glucose-1-P to ADP-Glc PPase

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Table 3

Role of Asp142 in ADP-Glc PPase

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Table 4

Amino acid substitutions in the ADP-Glc PPase allosteric mutant strains

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Table 5

Kinetic parameters of wild-type and mutant glycogen synthases

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Table 6

Comparison of primary structures of various BEs in the four best-conserved regions in the α-amylase family

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4
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Table 7

Genes involved in glycogen metabolism in

Citation: Preiss J. 2009. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2009; doi:10.1128/ecosalplus.4.7.4

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