Biosynthesis of bacterial glycogen. Kinetic studies of a glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) from a glycogen-deficient mutant of Escherichia coli B.

Preiss, Jack; Greenberg, Elaine; Sabraw, Annemiek

doi:10.1016/s0021-9258(19)40862-4

Cited by 56 publications

(3 citation statements)

References 39 publications

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“…Maize amylopectin (amylose free) and potato amylose (amylopectin free) were purchased from Calbiochem, Los Angeles, Calif.; potato amylose (average dp = 300) was from Nutritional Biochemical Co., Cleveland, Ohio; rabbit liver glycogen and rabbit muscle phosphorylase a were from Sigma, St. Louis, Mo. ; hog pancreatic -amylase (iP^FP'-treated, 640 U/mg) was from Worthington, Freehold, N.J.; and pullulanase was from Boehringer-Mannheim Corp., New York, N.Y. E. coli glycogen was isolated as previously described (Preiss et al, 1975).…”

Section: Methodsmentioning

confidence: 99%

Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase

Boyer¹,

Preiss²

1977

Biochemistry

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Section: Methodsmentioning

confidence: 99%

Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase

Boyer¹,

Preiss²

1977

Biochemistry

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“…; potato amylose (average DP-300) from Nutritional Biochemical Co., Cleveland, Ohio; hog pancreatic aamylase (DFP-treated; 640 U/mg) from Worthington, Freehold, N.J. Malto oligosaccharides [degree of polymerization 2-9] were prepared from amylose by partial acid hydrolysis and isolated by paper chromatography (Ough, 1964). E. coli B glycogen was isolated as previously described (Preiss et al, 1975). 3-Aminopropyl-, 4-amino- butyl-and 6-aminohexyl-Sepharose columns were prepared as described by Shaltiel and Er-El (1973).…”

Section: Methodsmentioning

confidence: 99%

Biosynthesis of bacterial glycogen. 13. Purification and properties of the Escherichia coli B ADPglucose: 1,4-α-D-glucan 4-α-glucosyltransferase

Fox¹,

Kawaguchi²,

Greenberg³

et al. 1976

Biochemistry

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The Escherichia coli B glycogen synthase has been purified to apparent homogeneity with the use of a 4-aminobutyl-Sepharose column. Two fractions of the enzyme were obtained: glycogen synthase I with a specific activity of 380 mumol mg-1 and devoid of branching enzyme activity and glycogen synthase II having a specific activity of 505 mumol mg-1 and containing branching enzyme activity which was 0.1% of the activity observed for the glycogen synthase. Only one protein band was found in disc gel electrophoresis for each glycogen synthase fraction and they were coincident with glycogen synthase activity. One major protein band and one very faint protein band which hardly moved into the gel were observed in sodium dodecyl sulfate gel electrophoresis of the glycogen synthase fractions. The subunit molecular weight of the major protein band in sodium dodecyl sulfate gel electrophoresis of both glycogen synthase fractions was determined to be 49 000 +/- 2 000. The molecular weights of the native enzymes were determined by sucrose density gradient ultracentrifugation. Glycogen synthase I had a molecular weight of 93 000 while glycogen synthase II had a molecular weight of 200 000. On standing at 4 degrees C or at -85 degrees C both enzymes transform into species having molecular weights of 98 000, 135 000, and 185 000. Thus active forms of the E. coli B glycogen synthase can exist as dimers, trimers, and tetramers of the subunit. The enzyme was shown to catalyze transfer of glucose from ADPglucose to maltose and to higher oligosaccharides of the maltodextrin series but not to glucose. 1,5-Gluconolactone was shown to be a potent inhibitor of the glycogen synthase reaction. The glycogen synthase reaction was shown to be reversible. Formation of labeled ADPglucose occurred from either [14C]ADP or [14C]glycogen. The ratio of ADP to ADPglucose at equilibrium at 37 degrees C was determined and was found to vary threefold in the pH range of 5.27-6.82. From these data the ratio of ADP2- to ADPglucose at equilibrium was determined to be 45.8 +/- 4.5. Assuming that deltaF degrees of the hydrolysis of the alpha-1,4-glucosidic linkage is -4.0 kcal the deltaF degrees of hydrolysis of the glucosidic linkage in ADPglucose is -6.3 kcal.

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“…Many organisms ranging from bacteria to eukaryotes accumulate carbon and energy in a specific form as reservoirs to prepare for harsh conditions such as temporary starvation (Preiss et al, 1975;Preiss, 1984). The most common form of energy and carbon storage can be divided into two groups: polysaccharides such as glycogen and starch, and lipids such as poly-β-hydroxybutyrate (Wilkinson, 1959(Wilkinson, , 1963.…”

Section: Introductionmentioning

confidence: 99%

Identification of the Genes Related to the Glycogen Metabolism in Hyperthermophilic Archaeon, Sulfolobus acidocaldarius

Lee

Bae²,

Park

et al. 2021

Front. Microbiol.

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Glycogen is a polysaccharide that comprises α-1,4-linked glucose backbone and α-1,6-linked glucose polymers at the branching points. It is widely found in organisms ranging from bacteria to eukaryotes. The physiological role of glycogen is not confined to being an energy reservoir and carbon source but varies depending on organisms. Sulfolobus acidocaldarius, a thermoacidophilic archaeon, was observed to accumulate granular glycogen in the cell. However, the role of glycogen and genes that are responsible for glycogen metabolism in S. acidocaldarius has not been identified clearly. The objective of this study is to identify the gene cluster, which is composed of enzymes that are predicted to be involved in the glycogen metabolism, and confirm the role of each of these genes by constructing deletion mutants. This study also compares the glycogen content of mutant and wild type and elucidates the role of glycogen in this archaeon. The glycogen content of S. acidocaldarius MR31, which is used as a parent strain for constructing the deletion mutant in this study, was increased in the early and middle exponential growth phases and decreased during the late exponential and stationary growth phases. The pattern of the accumulated glycogen was independent to the type of supplemented sugar. In the comparison of the glycogen content between the gene deletion mutant and MR31, glycogen synthase (GlgA) and α-amylase (AmyA) were shown to be responsible for the synthesis of glycogen, whereas glycogen debranching enzyme (GlgX) and glucoamylase (Gaa) appeared to affect the degradation of glycogen. The expressions of glgC–gaa–glgX and amyA–glgA were detected by the promoter assay. This result suggests that the gradual decrease of glycogen content in the late exponential and stationary phases occurs due to the increase in the gene expression of glgC–gaa–glgX. When the death rate in nutrient limited condition was compared among the wild type strain, the glycogen deficient strain and the strain with increased glycogen content, the death rate of the glycogen deficient strain was found to be higher than any other strain, thereby suggesting that the glycogen in S. acidocaldarius supports cell maintenance in harsh conditions.

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Biosynthesis of bacterial glycogen. Kinetic studies of a glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) from a glycogen-deficient mutant of Escherichia coli B.

Cited by 56 publications

References 39 publications

Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase

Biosynthesis of bacterial glycogen. Purification and properties of the Escherichia coli B α-1,4-glucan:α-1,4-glucan 6-glycosyltransferase

Biosynthesis of bacterial glycogen. 13. Purification and properties of the Escherichia coli B ADPglucose: 1,4-α-D-glucan 4-α-glucosyltransferase

Identification of the Genes Related to the Glycogen Metabolism in Hyperthermophilic Archaeon, Sulfolobus acidocaldarius

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