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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 13 May 2014 Accepted 10 October 2014 Published 19 December 2014
  • Address correspondence to Jack Preiss, preiss@msu.edu
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  • Abstract:

    Glycogen accumulation 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 because of the lack of a growth nutrient, e.g., a nitrogen source. This review describes the enzymatic reactions involved in glycogen synthesis and the allosteric regulation of the first enzyme, ADP-glucose pyrophosphorylase. The properties of the enzymes involved in glycogen synthesis, ADP-glucose pyrophosphorylase, glycogen synthase, and branching enzyme are also characterized. The data describing the genetic regulation of the glycogen synthesis are also presented. An alternate pathway for glycogen synthesis in mycobacteria is also described.

  • Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014

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Article Version

This article is an updated version of the following content:

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148. journal-id:
ecosalplus.ESP-0015-2014.citations
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/content/journal/ecosalplus/10.1128/ecosalplus.ESP-0015-2014
2014-12-19
2017-03-26

Abstract:

Glycogen accumulation 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 because of the lack of a growth nutrient, e.g., a nitrogen source. This review describes the enzymatic reactions involved in glycogen synthesis and the allosteric regulation of the first enzyme, ADP-glucose pyrophosphorylase. The properties of the enzymes involved in glycogen synthesis, ADP-glucose pyrophosphorylase, glycogen synthase, and branching enzyme are also characterized. The data describing the genetic regulation of the glycogen synthesis are also presented. An alternate pathway for glycogen synthesis in mycobacteria is also described.

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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. doi:10.1128/ecosalplus.ESP-0015-2014.f1

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Figure 2

Amino acids are represented by the one-letter amino acid code. Only those amino acids that are different in the serovar 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 ( 57 ), R67 is replaced by Cys in the allosteric mutant CL1136 enzyme ( 58 ), and Y114 has been shown to be involved in the binding of the substrate ATP ( 46 ) and the inhibitor AMP ( 39 , 40 ). D142 has been identified as being involved in catalysis ( 22 ). K195 has been shown to be involved in the binding of the substrate glucose-1-P ( 21 ), P295 is replaced by Ser in the allosteric mutant SG5 enzyme ( 59 ), and G336 is replaced by Asp in the allosteric mutant 618 enzyme ( 32 , 33 , 60 ). All these amino acids are conserved in the serovar Typhimurium ADP-Glc PPase. doi:10.1128/ecosalplus.ESP-0015-2014.f2

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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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. doi:10.1128/ecosalplus.ESP-0015-2014.f3

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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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. doi:10.1128/ecosalplus.ESP-0015-2014.f4

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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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 the 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). doi:10.1128/ecosalplus.ESP-0015-2014.f5

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Figure 6

This map was constructed from the sequences obtained from references 43 , 75 , 79 , 84 , 85 , 98 , and 99 . 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. doi:10.1128/ecosalplus.ESP-0015-2014.f6

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Figure 7

The site was detected by DNase I protection analysis ( 111 ), and that of serovar Typhimurium was derived on the basis of homology to the sequence ( 113 ). The asterisks indicate the conservation in the sequences of the transcripts with the consensus CRP binding site. doi:10.1128/ecosalplus.ESP-0015-2014.f7

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Figure 8

The 5′ termini of transcripts are indicated by asterisks, and the best −10 and −35 regions are underlined. doi:10.1128/ecosalplus.ESP-0015-2014.f8

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Figure 9

The CRP binding region was located by mobility shift analysis ( 111 ). Transcripts from wild-type strains of B and K-12 and isogenic glycogen synthesis mutants were examined by S1 nuclease protection analysis ( 111 ). doi:10.1128/ecosalplus.ESP-0015-2014.f9

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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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. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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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. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Table 3

Role of Asp142 in ADP-Glc PPase

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Table 4

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

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Table 5

Kinetic parameters of wild-type and mutant glycogen synthases

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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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. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014
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Table 7

Genes involved in glycogen metabolism in

Citation: Preiss J. 2014. Glycogen: Biosynthesis and Regulation, EcoSal Plus 2014; doi:10.1128/ecosalplus.ESP-0015-2014

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