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

Fox, Jeffrey L.; Kawaguchi, K.; Greenberg, Elaine; Preiss, Jack

doi:10.1021/bi00649a019

Cited by 66 publications

(42 citation statements)

References 51 publications

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“…Potassium fluoride and acetate have the reverse effect of being able to stimulate synthesis of protein-bound glycogen while not affecting glucose incorporation into added glycogen. The lack of effect of gluconolactone on the synthesis of acid-insoluble or soluble glycogen is to be contrasted with its total inhibition of ratliver [I71 and Escherichia coli glycogen synthases [18] and starch synthase [19].…”

Section: Distinction Between Mechanisms Of Incorporation Of [I4c]glucmentioning

confidence: 99%

The initation of glycogen biosynthesis in rat heart

Blumenfeld

Whelan

Krisman

1983

European Journal of Biochemistry

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A rat heart extract synthesizes glycogen‐like material from UDP‐glucose in the absence of added primer. Most of this material is precipitable by dilute trichloroacetic acid, in contrast to glycogen synthesized in presence of added glycogen primer. It is postulated that the endogenous initiation of glycogen synthesis occurs by apposition of glucose residues to a protein and that the material so synthesized in vitro corresponds to the protein‐bound glycogen reported to exist in rat heart. The ability to label the putative protein primer in vitro with [14C]glucose should assist the isolation of the primer and the elucidation of the nature of the association between the carbohydrate and protein moeities.

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Section: Distinction Between Mechanisms Of Incorporation Of [I4c]glucmentioning

confidence: 99%

The initation of glycogen biosynthesis in rat heart

Blumenfeld

Whelan

Krisman

1983

European Journal of Biochemistry

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“…Likewise, citrate was found to lower the K, of Escherichia coli glycogen synthase for glycogen 11-to 15-fold (8). Critical characterization of the E. coli enzyme showed that it contained large amounts of endogenous primer (4), thus possibly accounting for the unprimed synthesis. The unprimed reaction catalyzed by the E. coli glycogen synthase was found to be influenced by endogenous primer and citrate concentration as well as by glycogen-branching enzyme (8).…”

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confidence: 97%

“…is enzym fratio has been purified about 1,000fold frm maize kernels for the eosrmnuitant amykAw-exseder (ae). Previous reports have shown glycogen and starch synthase fractions from a number of sources catalyze a-glucan synthesis in the absence of added primer, when in the presence of high concentrations of citrate (4,6,8). This reaction has been termed "unprimed" starch and glycogen synthesis.…”

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confidence: 99%

Properties of Citrate-stimulated Starch Synthesis Catalyzed by Starch Synthase I of Developing Maize Kernels

Boyer

Preiss²

1979

Plant Physiol.

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Chromtography of extracts of maize on diethylaminoethyl-celllose resolvestarc synthae avity into two frcio (Ozbum, Hawker, Preiss 1971 Plant Physlo 4& 785-769). Only starc synthase I is capble of synthesis in the absece of added primer and the presene of 0.5 molar citrate. is enzym fratio has been purified about 1,000fold frm maize kernels for the eosrmnuitant amykAw-exseder (ae). Previous reports have shown glycogen and starch synthase fractions from a number of sources catalyze a-glucan synthesis in the absence of added primer, when in the presence of high concentrations of citrate (4,6,8). This reaction has been termed "unprimed" starch and glycogen synthesis. Citrate (0.5 M) was found to lower the Km ofthe unprimed spinach leafstarch synthase 3,400-fold for glycogen and 270-fold for amylopectin (6 Two fractions of starch synthase have been isolated from maize endosperm by DEAE-cellulose chromatography (10). Starch synthase I is able to catalyze unprimed glucan synthesis in the presence of high citrate concentration whereas starch synthase II is inactive under these conditions. In addition, starch synthase I had greater activity with glycogen than with amylopectin as primer, while starch synthase II had greater activity with amylopectin. Schiefer et al. (13) showed that treatment of a starch synthase from sweet corn with a-amylase abolished the unprimed starch synthesis activity and suggested that primer had been removed. However, they were unable to characterize fully the high citrate reaction, because their preparations were contaminated with branching enzyme. The purpose of this report is to describe the properties of the citrate-stimulated starch synthase reaction of maize endosperm. The purification of starch synthase I virtually free of branching enzyme activity was made possible by using endosperm extracts of the branching enzyme mutant amyloseextender. A preliminaqr report of some of this work has already appeared (I 1). MATERIALS AND METHODS MATERLUSThe dent maize (Zea mays L.) inbred W64A and inbred W64A homozygous for the endosperm mutant amylose-extender (ae) were field grown in 1976. Plants were self-or sib-pollinated and ears were harvested at 22 days after pollination, quick frozen in dry ice, and stored at -15 C until used. ADP-['4Cjglucose was prepared enzymically (12). Maize amylopectin (amylose-free) was purchased from Calbiochem; glycogen, ,B-amylase, and rabbit muscle phosphorylase a were obtained from Sigma. AminoalkylSepharose resin was prepared by the procedures of . All other reagents were of the highest purity available.PURICATION OF ADP-GLUCOSE -STARCH SYNTHASE Kernels (230 g) were ground with a porcelain mortar and pestle in the presence of 100 ml of cold 50 mm Tris-acetate buffer (pH 7.5) containing 2.5 mm DTT and 10 mm EDTA. Incompletely ground endosperm and pericarp material was collected by passing the homogenate through five layers of cheesecloth and the grinding repeated two additional times. This extracted solution constituted the crude extract. AM additional proce...

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“…The biosynthesis of glycogen requires three enzymes, ADPglucose pyrophosphorylase (EC 2.7.7.27), glycogen synthase (EC 2.4.1.21), and glycogen branching enzyme (EC 2.4.1.18), which are encoded by gigC, gigA, and gigB, respectively. The enzymes have been previously purified (9,20,27,28). The genes have been cloned on a single 10.5-kilobase (kb) genomic fragment (41), and their nucleotide sequences have been determined (4,5,35).…”

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Genetic regulation of glycogen biosynthesis in Escherichia coli: in vitro effects of cyclic AMP and guanosine 5'-diphosphate 3'-diphosphate and analysis of in vivo transcripts

1989

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Glycogen accumulation in Escherichia coli is inversely related to the growth rate and occurs most actively when cells enter the stationary phase. The levels of the three biosynthetic enzymes undergo corresponding changes under these conditions, suggesting that genetic control of enzyme biosynthesis may account for at least part of the regulation (J. Preiss, Annu. Rev. Microbiol. 38:419-458, 1984). We have begun to explore the molecular basis of this control by identifying factors which affect the expression of the glycogen genes and by determining the 5'-flanking regions required to mediate the regulatory effects. The in vitro coupled transcription-translation of two of the biosynthetic genes, glgC (ADPglucose pyrophosphorylase) and gigA (glycogen synthase), was enhanced up to 26-and 10-fold, respectively, by cyclic AMP (cAMP) and cAMP receptor protein (CRP). Guanosine 5'-diphosphate 3'-diphosphate stimulated the expression of these genes 3.6-and 1.8-fold, respectively. The expression of glgB (glycogen branching enzyme) was affected weakly or negligibly by the above-mentioned compounds. Assays which measured the in vitro formation of the first dipeptide of glgC showed that a restriction fragment which contained 0.5 kilobases of DNA upstream from the initiation codon supported cAMP-CRP-activated expression. Sequence-specific binding of cAMP-CRP to a 243-base-pair restriction fragment from the region upstream from glgC was observed by virtue of the altered electrophoretic mobility of the bound DNA. Sl nuclease protection analysis identffied 5' termini of four in vivo transcripts within 0.5 kilobases of the glgC coding region. The relative concentrations of transcripts were higher in the early stationary phase than in the exponential phase. Two mutants which overproduced the biosynthesis enzymes accumulated elevated levels 'of specific transcripts. The 5' termini of three of the transcripts were mapped to a high resolution. Their upstream sequences showed weak similarity to the E. coli consensus promoter. These results suggest complex transcriptional regulation of the glycogen biosynthesis genes involving multiple promoter sites and direct control of gene expression by at least two global regulatory systems.

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

Cited by 66 publications

References 51 publications

The initation of glycogen biosynthesis in rat heart

The initation of glycogen biosynthesis in rat heart

Properties of Citrate-stimulated Starch Synthesis Catalyzed by Starch Synthase I of Developing Maize Kernels

Genetic regulation of glycogen biosynthesis in Escherichia coli: in vitro effects of cyclic AMP and guanosine 5'-diphosphate 3'-diphosphate and analysis of in vivo transcripts

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