COMPARATIVE REGULATION OF Α1, 4-Glucan SYNTHESIS IN PHOTOSYNTHETIC AND NON-PHOTOSYNTHETIC SYSTEMS

Preiss, Jack; Kappel, William K.; Greenberg, Elaine

doi:10.1016/b978-0-12-066250-0.50014-4

Cited by 3 publications

(10 citation statements)

References 61 publications

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“…A high ratio increases the rate of starch accumulation while a low ratio appears to favor degradation (8,10). Consistent with this have been the findings that plant, algal, and cyanobacterial ADPglucose pyrophosphorylases are activated by 3-P-glycerate and inhibited by Pi (5,(17)(18)(19)21). Under the conditions approximating the in vivo or in situ concentrations of various metabolites reported to occur in spinach chloroplasts in light and dark conditions, the ADPglucose pyrophosphorylase is more sensitive to Pi inhibition in the dark conditions (Fig.…”

Section: Purification Of Adpglucose Pyrophosphorylase From Spinachsupporting

confidence: 74%

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Purification of Spinach Leaf ADPglucose Pyrophosphorylase

Copeland

Preiss²

1981

Plant Physiol.

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ADPglucose pyroposporylase from spinach leaves has been purified to homogeneity by hydrophobic chromatography cardied out in 1 molar phosphate buffer. After polyacrylamide gel electrophoresis, the preparation showed only one protein staining band that coincided with a single activity stain. The enzyme appears to be composed of two subunits with molecular weights of 44,000 and 48,000, respectively, as determined by SDS polyacrylamide gel electrophoresis. Thus ADPglucose pyrophosphorylase of spinach appears to be comprised of subunits which are similar in size to the subunits of ADPglucose pyrophosphorylase isolated from bacterial sources. In contrast, a subunit molecular weight of 96,000 has been reported for the maize endosperm ADPglucose pyrophosphorylase (Fuchs RL and JO Smith 1979 Biochim Biophys Acta 556: 40-48). The purified enzyme retains similar aflosteric and catalytic properties as reported previously and is more sensitive to phosphate inhibition under "dark"-sinulated conditions than under "light"-simulated conditions.The synthesis of ADPglucose from ATP and glucose-l-P, catalyzed by ADPglucose pyrophosphorylase (glucose-1-P adenylyl transferase, E.C. 2.2.7.27), is one of the main regulatory steps in the biosynthesis of starch in plants (5,18,22) and glycogen in bacteria (7,13,17,19). Extensive studies have been carried out on the kinetic and regulatory properties of ADPglucose pyrophosphorylase from a wide range of sources and these have been reviewed recently (17). The enzyme has been purified to homogeneity from several bacteria and the chemical and physical properties investigated. A mol wt of 185,000 has been found for ADPglucose pyrophosphorylase from Escherichia coli and the enzyme shows only one protein band of 50,000 mol wt following SDS-polyacrylamide electrophoresis (7). A mol wt of approximately 200,000 has been found for ADPglucose pyrophosphorylase from a number of other sources (13), including spinach leaves (21) and maize endosperm (6). In another report it has been suggested that the ADPglucose pyrophosphorylase of maize endosperm occurs in two forms, with mol wts of 200,000 and 400,000, with the subunit mol wt of the maize enzyme being 96,000 (3). It would therefore be of high interest to know the subunit molecular weight of other plant ADPglucose pyrophosphorylases, particularly those very sensitive to activation and inhibition by various effector molecules.ADPglucose pyrophosphorylase from spinach leaves has been previously purified to a high degree using preparative gel electro- phoresis (21) but this method has several disadvantages. A new purification procedure which includes a hydrophobic chromatography step carried out in 1 M phosphate buffer is described herein for ADPglucose pyrophosphorylase from spinach leaves. MATERIALS AND METHODSReagents. ['4C]Glucose-l-P and PPi-32P were obtained from New England Nuclear. Insoluble PVP obtained from Sigma was washed by boiling for 10 min in 10%o HCI and then washed with H20 until the pH of the wash reached 7.0. 3-Aminopropyl-Sep...

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Section: Purification Of Adpglucose Pyrophosphorylase From Spinachsupporting

confidence: 74%

“…2.2.7.27), is one of the main regulatory steps in the biosynthesis of starch in plants (5,18,22) and glycogen in bacteria (7,13,17,19). Extensive studies have been carried out on the kinetic and regulatory properties of ADPglucose pyrophosphorylase from a wide range of sources and these have been reviewed recently (17).…”

Section: Introductionmentioning

confidence: 99%

Purification of Spinach Leaf ADPglucose Pyrophosphorylase

Copeland

Preiss²

1981

Plant Physiol.

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“…Asp-Ser-Arg-Pho-Ile-Ser-(GIx )-Leu-X-Arg -(Asn) -X -Phe-Ala-Mot-Val FIG. 2. Comparison of N-terminal amino acid sequence of ADPglucose synthetases from E. coli (9,24), S. typhimurium (16), R. tenue (29), and R. sphaeroides. significant amount of phenylthiohydantoin amino acid was detected by gas chromatography, thin-layer chromatography, or high-pressure liquid chromatography.…”

Section: Resultsmentioning

confidence: 99%

“…ADPglucose, the sugar nucleotide involved in the synthesis of bacterial glycogen and plant starch, is synthesized from ATP and a-glucose-1-P in a reaction catalyzed by ADPglucose synthetase (EC 2.7.7.27) (20). With few exceptions, ADPglucose synthetase from these sources is allosterically activated by glycolytic intermediates and allosterically inhibited by 5'-AMP, 5'-ADP, or Pi (20)(21)(22)24). The enzyme appears to be regulated by the energy charge state of the cell (2) and requires the presence of glycolytic intermediates for full activity.…”

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Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase

Yung¹,

Preiss²

1982

J Bacteriol

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ADPglucose synthetase from the photosynthetic bacterium Rhodopseudomonas sphaeroides was purified to greater than 95% purity. The molecular weight of the R. sphaeroides enzyme, as determined by sucrose density gradient ultracentrifugation, was approximately 204,000. The subunit molecular weight of the enzyme based on sodium dodecyl sulfate-gel electrophoresis was 46,000. Although the amino acid composition of the enzyme was similar to that found for the enzymes from Escherichia coli, Salmonella typhimurium, and Rhodospirillum tenue, no apparent homology has been observed between the N-terminal or Cterminal amino acid sequences. Antisera prepared against the ADPglucose synthetase could inhibit the activities of the enzyme from other photosynthetic bacteria. Therefore, some sequence homology may exist within the internal portion of their peptide chain.

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Biosynthesis of bacterial glycogen: purification and structural properties of Rhodospirillum tenue adenosine diphosphate glucose synthetase

Yung¹,

Preiss²

1981

J Bacteriol

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Adenosine diphosphate glucose synthetase from the photosynthetic bacterium Rhodospirillum tenue has been purified greater than 95%. The molecular weight of the enzyme is approximately 215,000, with a subunit molecular weight of about 51,000. The enzyme appears to be composed of four similar if not identical subunits. Although the amino acid composition of the enzyme is similar to that of Escherichia coli and Salmonella typhimurium, no apparent homology has been observed between their N-terminal amino acid sequences. Antisera prepared against the R. tenue enzyme can partially inhibit the activities of adenosine diphosphate glucose synthetases from other photosynthetic bacteria.

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COMPARATIVE REGULATION OF Α1, 4-Glucan SYNTHESIS IN PHOTOSYNTHETIC AND NON-PHOTOSYNTHETIC SYSTEMS

Cited by 3 publications

References 61 publications

Purification of Spinach Leaf ADPglucose Pyrophosphorylase

Purification of Spinach Leaf ADPglucose Pyrophosphorylase

Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase

Biosynthesis of bacterial glycogen: purification and structural properties of Rhodospirillum tenue adenosine diphosphate glucose synthetase

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